Relevant bibliographies by topics / Lipids Membrane proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Lipids Membrane proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "Lipids Membrane proteins"

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Corey, Robin A., Phillip J. Stansfeld, and Mark S. P. Sansom. "The energetics of protein–lipid interactions as viewed by molecular simulations." Biochemical Society Transactions 48, no. 1 (December 24, 2019): 25–37. http://dx.doi.org/10.1042/bst20190149.

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Membranes are formed from a bilayer containing diverse lipid species with which membrane proteins interact. Integral, membrane proteins are embedded in this bilayer, where they interact with lipids from their surroundings, whilst peripheral membrane proteins bind to lipids at the surface of membranes. Lipid interactions can influence the function of membrane proteins, either directly or allosterically. Both experimental (structural) and computational approaches can reveal lipid binding sites on membrane proteins. It is, therefore, important to understand the free energies of these interactions. This affords a more complete view of the engagement of a particular protein with the biological membrane surrounding it. Here, we describe many computational approaches currently in use for this purpose, including recent advances using both free energy and unbiased simulation methods. In particular, we focus on interactions of integral membrane proteins with cholesterol, and with anionic lipids such as phosphatidylinositol 4,5-bis-phosphate and cardiolipin. Peripheral membrane proteins are exemplified via interactions of PH domains with phosphoinositide-containing membranes. We summarise the current state of the field and provide an outlook on likely future directions of investigation.
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Renard, Kenta, and Bernadette Byrne. "Insights into the Role of Membrane Lipids in the Structure, Function and Regulation of Integral Membrane Proteins." International Journal of Molecular Sciences 22, no. 16 (August 21, 2021): 9026. http://dx.doi.org/10.3390/ijms22169026.

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Membrane proteins exist within the highly hydrophobic membranes surrounding cells and organelles, playing key roles in cellular function. It is becoming increasingly clear that the membrane does not just act as an appropriate environment for these proteins, but that the lipids that make up these membranes are essential for membrane protein structure and function. Recent technological advances in cryogenic electron microscopy and in advanced mass spectrometry methods, as well as the development of alternative membrane mimetic systems, have allowed experimental study of membrane protein–lipid complexes. These have been complemented by computational approaches, exploiting the ability of Molecular Dynamics simulations to allow exploration of membrane protein conformational changes in membranes with a defined lipid content. These studies have revealed the importance of lipids in stabilising the oligomeric forms of membrane proteins, mediating protein–protein interactions, maintaining a specific conformational state of a membrane protein and activity. Here we review some of the key recent advances in the field of membrane protein–lipid studies, with major emphasis on respiratory complexes, transporters, channels and G-protein coupled receptors.
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Torres, Manuel, Catalina Ana Rosselló, Paula Fernández-García, Victoria Lladó, Or Kakhlon, and Pablo Vicente Escribá. "The Implications for Cells of the Lipid Switches Driven by Protein–Membrane Interactions and the Development of Membrane Lipid Therapy." International Journal of Molecular Sciences 21, no. 7 (March 27, 2020): 2322. http://dx.doi.org/10.3390/ijms21072322.

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The cell membrane contains a variety of receptors that interact with signaling molecules. However, agonist–receptor interactions not always activate a signaling cascade. Amphitropic membrane proteins are required for signal propagation upon ligand-induced receptor activation. These proteins localize to the plasma membrane or internal compartments; however, they are only activated by ligand-receptor complexes when both come into physical contact in membranes. These interactions enable signal propagation. Thus, signals may not propagate into the cell if peripheral proteins do not co-localize with receptors even in the presence of messengers. As the translocation of an amphitropic protein greatly depends on the membrane’s lipid composition, regulation of the lipid bilayer emerges as a novel therapeutic strategy. Some of the signals controlled by proteins non-permanently bound to membranes produce dramatic changes in the cell’s physiology. Indeed, changes in membrane lipids induce translocation of dozens of peripheral signaling proteins from or to the plasma membrane, which controls how cells behave. We called these changes “lipid switches”, as they alter the cell’s status (e.g., proliferation, differentiation, death, etc.) in response to the modulation of membrane lipids. Indeed, this discovery enables therapeutic interventions that modify the bilayer’s lipids, an approach known as membrane-lipid therapy (MLT) or melitherapy.
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Booth, Paula J., A. Rachael Curran, Richard H. Templer, Hui Lu, and Wim Meijberg. "Manipulating the folding of membrane proteins: using the bilayer to our advantage." Biochemical Society Symposia 68 (August 1, 2001): 27–33. http://dx.doi.org/10.1042/bss0680027.

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The folding mechanisms of integral membrane proteins have largely eluded detailed study. This is owing to the inherent difficulties in folding these hydrophobic proteins in vitro, which, in turn, reflects the often apparently insurmountable problem of mimicking the natural membrane bilayer with lipid or detergent mixtures. There is, however, a large body of information on lipid properties and, in particular, on phosphatidylcholine and phosphatidylethanolamine lipids, which are common to many biological membranes. We have exploited this knowledge to develop efficient in vitro lipid-bilayer folding systems for the membrane protein, bacteriorhodopsin. Furthermore, we have shown that a rate-limiting apoprotein folding step and the overall folding efficiency appear to be controlled by particular properties of the lipid bilayer. The properties of interest are the stored curvature elastic energy within the bilayer, and the lateral pressure that the lipid chains exert on the their neighbouring folding proteins. These are generic properties of the bilayer that can be achieved with simple mixtures of biological lipids, and are not specific to the lipids studied here. These bilayer properties also seem to be important in modulating the function of several membrane proteins, as well as the function of membranes in vivo. Thus, it seems likely that careful manipulations of lipid properties will shed light on the forces that drive membrane protein folding, and will aid the development of bilayer folding systems for other membrane proteins.
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Levi, Valeria, Ana M. Villamil Giraldo, Pablo R. Castello, Juan P. F. C. Rossi, and F. Luis González Flecha. "Effects of phosphatidylethanolamine glycation on lipid–protein interactions and membrane protein thermal stability." Biochemical Journal 416, no. 1 (October 28, 2008): 145–52. http://dx.doi.org/10.1042/bj20080618.

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Non-enzymatic glycation of biomolecules has been implicated in the pathophysiology of aging and diabetes. Among the potential targets for glycation are biological membranes, characterized by a complex organization of lipids and proteins interacting and forming domains of different size and stability. In the present study, we analyse the effects of glycation on the interactions between membrane proteins and lipids. The phospholipid affinity for the transmembrane surface of the PMCA (plasma-membrane Ca2+-ATPase) was determined after incubating the protein or the phospholipids with glucose. Results show that the affinity between PMCA and the surrounding phospholipids decreases significantly after phosphospholipid glycation, but remains unmodified after glycation of the protein. Furthermore, phosphatidylethanolamine glycation decreases by ∼30% the stability of PMCA against thermal denaturation, suggesting that glycated aminophospholipids induce a structural rearrangement in the protein that makes it more sensitive to thermal unfolding. We also verified that lipid glycation decreases the affinity of lipids for two other membrane proteins, suggesting that this effect might be common to membrane proteins. Extending these results to the in vivo situation, we can hypothesize that, under hyperglycaemic conditions, glycation of membrane lipids may cause a significant change in the structure and stability of membrane proteins, which may affect the normal functioning of membranes and therefore of cells.
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Hunte, C. "Specific protein–lipid interactions in membrane proteins." Biochemical Society Transactions 33, no. 5 (October 26, 2005): 938–42. http://dx.doi.org/10.1042/bst0330938.

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Many membrane proteins selectively bind defined lipid species. This specificity has an impact on correct insertion, folding, structural integrity and full functionality of the protein. How are these different tasks achieved? Recent advances in structural research of membrane proteins provide new information about specific protein–lipid interactions. Tightly bound lipids in membrane protein structures are described and general principles of the binding interactions are deduced. Lipid binding is stabilized by multiple non-covalent interactions from protein residues to lipid head groups and hydrophobic tails. Distinct lipid-binding motifs have been identified for lipids with defined head groups in membrane protein structures. The stabilizing interactions differ between the electropositive and electronegative membrane sides. The importance of lipid binding for vertical positioning and tight integration of proteins in the membrane, for assembly and stabilization of oligomeric and multisubunit complexes, for supercomplexes, as well as for functional roles are pointed out.
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Corey, Robin A., Wanling Song, Anna L. Duncan, T. Bertie Ansell, Mark S. P. Sansom, and Phillip J. Stansfeld. "Identification and assessment of cardiolipin interactions with E. coli inner membrane proteins." Science Advances 7, no. 34 (August 2021): eabh2217. http://dx.doi.org/10.1126/sciadv.abh2217.

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Integral membrane proteins are localized and/or regulated by lipids present in the surrounding bilayer. While bacteria have relatively simple membranes, there is ample evidence that many bacterial proteins bind to specific lipids, especially the anionic lipid cardiolipin. Here, we apply molecular dynamics simulations to assess lipid binding to 42 different Escherichia coli inner membrane proteins. Our data reveal an asymmetry between the membrane leaflets, with increased anionic lipid binding to the inner leaflet regions of the proteins, particularly for cardiolipin. From our simulations, we identify >700 independent cardiolipin binding sites, allowing us to identify the molecular basis of a prototypical cardiolipin binding site, which we validate against structures of bacterial proteins bound to cardiolipin. This allows us to construct a set of metrics for defining a high-affinity cardiolipin binding site on bacterial membrane proteins, paving the way for a heuristic approach to defining other protein-lipid interactions.
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Lee, Anthony G. "Lipid–protein interactions." Biochemical Society Transactions 39, no. 3 (May 20, 2011): 761–66. http://dx.doi.org/10.1042/bst0390761.

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Intrinsic membrane proteins are solvated by a shell of lipid molecules interacting with the membrane-penetrating surface of the protein; these lipid molecules are referred to as annular lipids. Lipid molecules are also found bound between transmembrane α-helices; these are referred to as non-annular lipids. Annular lipid binding constants depend on fatty acyl chain length, but the dependence is less than expected from models based on distortion of the lipid bilayer alone. This suggests that hydrophobic matching between a membrane protein and the surrounding lipid bilayer involves some distortion of the transmembrane α-helical bundle found in most membrane proteins, explaining the importance of bilayer thickness for membrane protein function. Annular lipid binding constants also depend on the structure of the polar headgroup region of the lipid, and hotspots for binding anionic lipids have been detected on some membrane proteins; binding of anionic lipid molecules to these hotspots can be functionally important. Binding of anionic lipids to non-annular sites on membrane proteins such as the potassium channel KcsA can also be important for function. It is argued that the packing preferences of the membrane-spanning α-helices in a membrane protein result in a structure that matches nicely with that of the surrounding lipid bilayer, so that lipid and protein can meet without either having to change very much.
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WANG, XUEJING, LEI WANG, XIAOJUN HAN, and CHANGJUN GUO. "MIGRATION OF CHARGED SPECIES IN LIPID BILAYER MEMBRANES UNDER AN ELECTRIC FIELD." Nano 08, no. 01 (February 2013): 1230006. http://dx.doi.org/10.1142/s179329201230006x.

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This paper reviews recent progress in studies on the migration of charged species, including charged lipids, membrane-attached proteins and vesicles, and integrated membrane proteins, in lipid bilayer membranes under an external electric field. The migration of these charged substances is controlled by the interplay of electrophoresis and electroosmosis. This phenomenon can be employed to separate the charged lipids and membrane-attached proteins, and concentrate integrated membrane proteins.
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Thompson, J. E., C. D. Froese, Y. Hong, K. A. Hudak, and M. D. Smith. "Membrane deterioration during senescence." Canadian Journal of Botany 75, no. 6 (June 1, 1997): 867–79. http://dx.doi.org/10.1139/b97-096.

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The lipid bilayers of plant membranes are normally liquid crystalline, reflecting the inherent rotational motion of membrane fatty acids at physiological temperature. With the onset of senescence, the chemical composition of membrane lipids changes resulting in lipid phase separations within the bilayer. These phase changes render the membranes leaky and lead to loss of essential ion gradients and impairment of cell function. The separation of lipid phases appears to be attributable to an accumulation of lipid metabolites in the bilayer that are formed during turnover and metabolism of membrane lipids. These metabolites are normally released from membranes as lipid–protein particles found in the cell cytosol and within organelles. The lipid–protein particles also contain catabolites of membrane proteins and appear to serve as a vehicle for removing lipid and protein metabolites that would otherwise destabilize the bilayer. They bear structural resemblance to oil bodies, which are abundant in oil seeds, and have been found in leaves, cotyledons, and petals as well as in insect and animal tissue. The accumulation of lipid metabolites in senescing membranes and ensuing separation of lipid phases appear to reflect impairment of lipid–protein particle release from membranes as tissues age and to be a seminal cause of membrane dysfunction with advancing senescence. Key words: lipid bilayer, lipid phase separation, lipid–protein particles, membrane, oil body, senescence.
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Dissertations / Theses on the topic "Lipids Membrane proteins"

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Oldham, Alexis Jean. "Modulation of lipid domain formation in mixed model systems by proteins and peptides." View electronic thesis, 2008. http://dl.uncw.edu/etd/2008-1/r1/oldhama/alexisoldham.pdf.

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Hubert, Anne Kasyoka. "Interactions between membrane transport proteins and lipids." Thesis, University of Leeds, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.432304.

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Ariöz, Candan. "Exploring the Interplay of Lipids and Membrane Proteins." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-102675.

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The interplay between lipids and membrane proteins is known to affect membrane protein topology and thus have significant effect (control) on their functions. In this PhD thesis, the influence of lipids on the membrane protein function was studied using three different membrane protein models. A monotopic membrane protein, monoglucosyldiacylglyecerol synthase (MGS) from Acholeplasma laidlawii is known to induce intracellular vesicles when expressed in Escherichia coli. The mechanism leading to this unusual phenomenon was investigated by various biochemical and biophysical techniques. The results indicated a doubling of lipid synthesis in the cell, which was triggered by the selective binding of MGS to anionic lipids. Multivariate data analysis revealed a good correlation with MGS production. Furthermore, preferential anionic lipid sequestering by MGS was shown to induce a different fatty acid modeling of E. coli membranes. The roles of specific lipid binding and the probable mechanism leading to intracellular vesicle formation were also investigated. As a second model, a MGS homolog from Synechocystis sp. PCC6803 was selected. MgdA is an integral membrane protein with multiple transmembrane helices and a unique membrane topology. The influence of different type of lipids on MgdA activity was tested with different membrane fractions of Synechocystis. Results indicated a very distinct profile compared to Acholeplasma laidlawii MGS. SQDG, an anionic lipid was found to be the species of the membrane that increased the MgdA activity 7-fold whereas two other lipids (PG and PE) had only minor effects on MgdA. Additionally, a working model of MgdA for the biosynthesis and flow of sugar lipids between Synechocystis membranes was proposed. The last model system was another integral membrane protein with a distinct structure but also a different function. The envelope stress sensor, CpxA and its interaction with E. coli membranes were studied. CpxA autophosphorylation activity was found to be positively regulated by phosphatidylethanolamine and negatively by anionic lipids. In contrast, phosphorylation of CpxR by CpxA revealed to be increased with PG but inhibited by CL. Non-bilayer lipids had a negative impact on CpxA phosphotransfer activity. Taken together, these studies provide a better understanding of the significance of the interplay of lipids and model membrane proteins discussed here.
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Danial, John Shokri Hanna. "Imaging lipid phase separation on droplet interface bilayers." Thesis, University of Oxford, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.711943.

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Polozov, Ivan V. "Interactions of class A and class L amphipathic helical peptides with model membranes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0006/NQ30110.pdf.

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Clogston, Jeffrey. "Applications of the lipidic cubic phase from controlled release and uptake to in meso crystallization of membrane proteins /." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1117564268.

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Thesis (Ph.D.)--Ohio State University, 2005.
Title from first page of PDF file. Document formatted into pages; contains xxii, 352 p.; also includes graphics. Includes bibliographical references (p. 346-352). Available online via OhioLINK's ETD Center
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Naughton, Fiona. "Interactions of perihperal membrane proteins with phosphatidylinositol lipids : insights from molecular dynamics simulations." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:d7bb7b03-3eda-40f2-85fc-f5a314ae3c44.

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Interactions between proteins and membranes are central to many signalling pathways and other cellular processes. Phosphatidylinositol phosphates (PIPs) are a family of lipids often acting as second messengers and targeted by peripheral proteins in these processes. A pipeline was developed combining the molecular dynamics (MD) approaches of umbrella sampling and coarse-grain modelling, and used to quantify and compare the interactions with PIP-containing model membranes of 13 pleckstrin homology (PH) domains, a common lipid-binding domain found in many proteins showing varied affinities and specificities for PIPs. Lipid selectivity generally agreed with previous observations. Several membrane-binding modes were identified, revealing PIP interactions through a secondary site are more common than suggested experimentally and appear to be related to overall affinity. Results suggest that simultaneous binding of multiple PIP lipids is required to achieve the high affinities characteristic of PH domains. Multiscale MD, combining coarse-grain binding simulations and atomistic refinement, was used to investigate PTEN, a tumour suppressor catalysing interconversion of PIPs and associated with many cancers and other disorders. Regions often ignored in previous studies were revealed to favour productive binding, largely via electrostatics. PIP clustering by bound PTEN and membrane insertion in the productive mode were demonstrated. Existence of an N-terminal PIP-binding site was supported, with this region appearing disordered, rather than helical as previously suggested. Changes in interdomain orientation when bound and with the clinically-relevant R173C mutation further suggest the importance of the interdomain interface for productive binding. Together, this work demonstrates the important contributions MD can make towards understanding protein/membrane interactions, particularly in the context of managing the diseases caused by their disruption.
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Nordlund, Gustav. "Membrane-mimetic systems : Novel methods and results from studies of respiratory enzymes." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-94554.

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The processes localized to biological membranes are of great interest, both from a scientific and pharmaceutical point of view. Understanding aspects such as the detailed mechanism and regulation of these processes requires investigation of the structure and function of the membrane-bound proteins in which they take place. The study of these processes is often complicated by the need to create in vitro systems that mimic the environment in which these proteins are normally found in vivo. This thesis describes some of the methods available for membrane-protein studies in membrane-mimetic systems, as well as our work aimed at developing such systems. Furthermore, results from studies using these systems are described. In the first two studies, described in Papers I & II, we investigated the use of silica particle-supported lipid bilayers, both for membrane-protein studies and as possible drug-delivery vehicles. Successful reconstitution of a multisubunit proton-pump, cytochrome c oxidase is described and characterized. Initial attempts to develop drug-delivery systems with two different targeting peptides are also described in the thesis. The second part of this thesis revolves around our work with membraneprotein dependent pathways. Results from studies of systems where the proton- pump bo3 oxidase and ATP synthase work in concert are described. The results show a surprising lipid-composition dependence for the coupled bo3- ATP-synthase activity (Paper III). Finally, a new system utilizing synaptic vesicle-fusion proteins for coreconstitution of membrane proteins is described, showing successful coreconstitution of a small respiratory chain, delivery of soluble proteins to preformed liposomes and reconstitution of ATP synthase in native membranes (Paper IV).

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Manuscript. Paper 4: Manuscript.

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Putta, Priya. "The Tale/ Head of Two Membrane Lipids Through Protein Interactions." Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1524311387080992.

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Mulet, Xavier. "Phosphatidylinositol Lipids and the role of Membrane Curvature in Regulation of Membrane-Associated Proteins." Thesis, Imperial College London, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.498508.

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Books on the topic "Lipids Membrane proteins"

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Kleinschmidt, Jörg H. Lipid-protein Interactions: Methods and protocols. New York: Humana Press, 2013.

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Membrane structural biology: With biochemical and biophysical foundations. Cambridge: Cambridge University Press, 2008.

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Graham, J. M. Membrane analysis. Oxford, UK: BIOS Scientific Publishers, 1997.

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Proteins: Membrane binding and pore formation. New York: Springer Science+Business Media, 2010.

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Les modèles moléculaires de biomembranes. Paris: Hermann, 1987.

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Miguel A. R. B. Castanho. Membrane-active peptides: Methods and results on structure and function. La Jolla, Calif: International University Line, 2009.

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Membrane-active peptides: Methods and results on structure and function. La Jolla, Calif: International University Line, 2009.

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L, Longo Marjorie, Risbud Subhash H, Jue Thomas, and SpringerLink (Online service), eds. Biomembrane Frontiers: Nanostructures, Models, and the Design of Life. Totowa, NJ: Humana Press, 2009.

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Membrane proteins: Folding, association, and design. New York: Humana Press, 2013.

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Jones, Malcolm N. Micelles, monolayers, and biomembranes. New York: Wiley-Liss, 1995.

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Book chapters on the topic "Lipids Membrane proteins"

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Masotti, L., J. Von Berger, and N. Gesmundo. "Conformational Changes in Polypeptides and Proteins Brought About by Interactions with Lipids." In Membrane Proteins, 95–106. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71543-3_11.

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Johns, Janet, and Arthur G. Szabo. "Reproducible Preparation of Phosphatidylserine Vesicles for Fluorescence Studies of Protein Incorporation into Lipids." In Membrane Proteins, 32–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71543-3_4.

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Lakey, Jeremy H., and Gregor Anderluh. "Membrane-Disrupting Proteins." In Biogenesis of Fatty Acids, Lipids and Membranes, 729–39. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-50430-8_53.

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Lakey, Jeremy H., and Gregor Anderluh. "Membrane-Disrupting Proteins." In Biogenesis of Fatty Acids, Lipids and Membranes, 1–11. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43676-0_53-1.

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Gong, Xiao-Min, Carla M. Franzin, Khang Thai, Jinghua Yu, and Francesca M. Marassi. "Nuclear Magnetic Resonance Structural Studies of Membrane Proteins in Micelles and Bilayers." In Methods in Membrane Lipids, 515–29. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-519-0_35.

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Bogdanov, Mikhail, Heidi Vitrac, and William Dowhan. "Flip-Flopping Membrane Proteins: How the Charge Balance Rule Governs Dynamic Membrane Protein Topology." In Biogenesis of Fatty Acids, Lipids and Membranes, 609–36. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-50430-8_62.

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Bogdanov, Mikhail, Heidi Vitrac, and William Dowhan. "Flip-Flopping Membrane Proteins: How the Charge Balance Rule Governs Dynamic Membrane Protein Topology." In Biogenesis of Fatty Acids, Lipids and Membranes, 1–28. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-43676-0_62-1.

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Sturgis, James N. "Building Model Membranes with Lipids and Proteins: Dangers and Challenges." In Membrane Proteins Production for Structural Analysis, 253–66. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0662-8_9.

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Ferguson, M. A. J. "Identification of Glycosyl-Phosphatidylinositol Membrane Anchors by Fatty Acid Labeling." In Post-translational Modification of Proteins by Lipids, 1–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74009-1_1.

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Hayashi, S., and H. C. Wu. "Identification and Characterization of Lipid-Modified Membrane Proteins in Bacteria." In Post-translational Modification of Proteins by Lipids, 88–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74009-1_16.

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Conference papers on the topic "Lipids Membrane proteins"

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Caffrey, Martin. "Lipid Phase Behavior: Databases, Rational Design and Membrane Protein Crystallization." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192724.

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The relationship that exists between structure and function is a unifying theme in my varied biomembrane-based research activities. It applies equally well to the lipid as to the protein component of membranes. With a view to exploiting information that has been and that is currently being generated in my laboratory, as well as that which exists in the literature, a number of web-accessible, relational databases have been established over the years. These include databases dealing with lipids, detergents and membrane proteins. Those catering to lipids include i) LIPIDAT, a database of thermodynamic information on lipid phases and phase transitions, ii) LIPIDAG, a database of phase diagrams concerning lipid miscibility, and iii) LMSD, a lipid molecular structures database. CMCD is the detergent-based database. It houses critical micelle concentration information on a wide assortment of surfactants under different conditions. The membrane protein data bank (MPDB) was established to provide convenient access to the 3-D structure and related properties of membrane proteins and peptides. The utility and current status of these assorted databases will be described and recommendations will be made for extending their range and usefulness.
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Creasy, M. Austin, and Donald J. Leo. "Modeling Bilayer Systems as Electrical Networks." In ASME 2010 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2010. http://dx.doi.org/10.1115/smasis2010-3791.

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Bilayers are synthetically made cell membranes that are used to study cell membrane properties or make functional devices that use the properties of the cell membrane components. Lipids and proteins are two of the main components of a cell membrane. Lipids are amphiphilic molecules that can self assemble into organized structures in the presences of water and this self assembly property can be used to form bilayers. Because of the amphiphilic nature of the lipids, a bilayer is impermeable to ion flow. Proteins are the active structures of a cell membrane that opens pores through the membrane for ions and other molecules to pass. Proteins are made from amino acids and have varying properties that depend on its configuration. Some proteins are activated by reactions (chemical, thermal, etc) or gradients induced across the bilayer. One way of testing bilayers to find bilayer properties is to induce a potential gradient across a membrane that induces ion flow and this flow can be measured as an electrical current. But, these pores may be voltage gated or activated by some other stimuli and therefore cannot be modeled as a linear conductor. Usually the conductance of the protein is a nonlinear function of the input that activates the protein. A small system that consists of a single bilayer and protein with few changing components can be easily modeled, but as systems become larger with multiple bilayers, multiple variables, and multiple proteins, the models will become more complex. This paper looks at how to model a system of multiple bilayers and the peptide alamethicin. An analytical expression for this peptide is used to match experimental data and a short study on the sensitivity of the variables is performed.
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Chen, Hsiu-hung Simon, Zhiquan Shu, Lei Cheng, and Dayong Gao. "Development of a Microfluidic Injection and Perfusion Device for Single Cell Study." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13317.

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The cell membrane, composed primarily of proteins and lipids, is a selectively permeable lipid bilayer in the scale of 10 nm or so. Molecules permeating through cell membranes play critical roles in the applications of drug delivery, cell therapy, and cryopreservation. Cryopreservation and banking of cells, such as umbilical cord bloods, female eggs, etc., are critical to facilitate practical and effective in vitro fertilization (IVF). The determination of molecule transport properties of cells, such as water and cryoprotectants (CPAs), is indispensable for developing optimal conditions for cryopreserving them. On the other hand, injection of material of interests, such as sperms and DNA segments, to female eggs or blastocysts, so-called intracytoplasmic sperm injection (ICSI) technique, are playing important roles on IVF and advanced gene knock-out. In this study, a novel micro-nano-fluidic system that allows perfusion and injection in nano-liter scale has been developed and fabricated by soft lithographic methods. A single cell in the microfluidic system is able to be trapped on site and then either be perfused by various solutions or injected with plain solutions or solutions with genetic materials. Our ongoing study will demonstrate that the micro-nano-fluidic system allows us to: 1) confine cells in a channel; 2) deliver drugs by perfusing the cell; 3) monitor osmotic behaviors of the cell by replacing its extracellular environment; and 4) perform ICSI with sperms or genetic materials.
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Chu, Benjamin, Dean Ho, Hyeseung Lee, Karen Kuo, and Carlo Montemagno. "Protein-Functionalized Proton Exchange Membranes." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46018.

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Protein-functionalized biomimetic membranes, based upon a triblock copolymer simulating a natural lipid bilayer in a single chain, serves as a core technology for applications in bioenergetics. Monolayers of block copolymer, which simulates the hydrophilic-hydrophobic-hydrophilic chain of a natural cell membrane, can be formed by Langmuir-Blodgett (LB) deposition and provides a favorable environment for protein refolding. Large-scale membrane formation is achieved using LB deposition on a variety of substrates, such as gold, quartz, silicon, and Nafion®. We have successfully inserted membrane proteins, such as the light-activated proton pump, bacteriorhodopsin (BR) and the pH/voltage-gateable porin, Outermembrane Protein F (OmpF), into large-area LB monolayers. We have also established sustained protein functionality in films through the measurement of light-activated proton transport.
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Lee, Hyeseung, Dean Ho, Benjamin Chu, Karen Kuo, and Carlo Montemagno. "Reconstituting Membrane Proteins Into Artificial Membranes and Detection of Their Activities." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46016.

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We have successfully purified BR from purple membrane of Halobacterium Salinarium and Cox from the genetically engineered plasmid inserted in Rhodobacter Sphaeroides. The activities of the purified enzymes have shown in lipid vesicles as well as in polymer vesicles and planar membranes. Phosphatidylcholine derived lipid vesicles created the most nature like environment for the enzymes. Triblock copolymer membrane was the alternative choice for membrane protein reconstitution since polymers are more durable, ideal for industrial applications and support enzyme activities better. We also demonstrated the backward function of Cox in vitro by changing proton concentration in the surrounding medium. Langmuir-Blodgett method was used to reconstitute the enzymes into the planar lipid or polymer membranes. The enzyme activities of the enzymes in planar membrane system were tested by impedance spectroscopy.
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Maftouni, Negin, Mehriar Amininasab, MohammadReza Ejtehadi, and Farshad Kowsari. "Multiscale Molecular Dynamics Simulation of Nanobio Membrane in Interaction With Protein." In ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/nemb2013-93054.

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One of the most important biological components is lipid nanobio membrane. The lipid membranes of alive cells and their mechanical properties play an important role in biophysical investigations. Some proteins affect the shape and properties of the nanobio membrane while interacting with it. In this study a multiscale approach is experienced: first a 100ns all atom (fine-grained) molecular dynamics simulation is done to investigate the binding of CTX A3, a protein from snake venom, to a phosphatidylcholine lipid bilayer, second, a 5 micro seconds coarse-grained molecular dynamics simulation is carried out to compute the pressure tensor, lateral pressure, surface tension, and first moment of lateral pressure. Our simulations reveal that the insertion of CTX A3 into one monolayer results in an asymmetrical change in the lateral pressure and distribution of surface tension of the individual bilayer leaflets. The relative variation in the surface tension of the two monolayers as a result of a change in the contribution of the various intermolecular forces may be expressed morphologically and lead to deformation of the lipid membrane.
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Lykotrafitis, George, and He Li. "Two-Component Coarse-Grain Model for Erythrocyte Membrane." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-62133.

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Biological membranes are vital components of living cells as they function to maintain the structural integrity of the cells. Red blood cell (RBC) membrane comprises the lipid bilayer and the cytoskeleton network. The lipid bilayer consists of phospholipids, integral membrane proteins, peripheral proteins and cholesterol. It behaves as a 2D fluid. The cytoskeleton is a network of spectrin tetramers linked at the actin junctions. It is connected to the lipid bilayer primarily via Band-3 and ankyrin proteins. In this paper, we introduce a coarse-grained model with high computational efficiency for simulating a variety of dynamic and topological problems involving erythrocyte membranes. Coarse-grained agents are used to represent a cluster of lipid molecules and proteins with a diameter on the order of lipid bilayer thickness and carry both translational and rotational freedom. The membrane cytoskeleton is modeled as a canonical exagonal network of entropic springs that behave as Worm-Like-Chains (WLC). By simultaneously invoking these characteristics, the proposed model facilitates simulations that span large length-scales (∼ μm) and time-scales (∼ ms). The behavior of the model under shearing at different rates is studied. At low strain rates, the resulted shear stress is mainly due to the spectrin network and it shows the characteristic non-linear behavior of entropic networks, while the viscosity of the fluid-like lipid bilayer contributes to the resulting shear stress at higher strain rates. The apparent ease of this model in combining the spectrin network with the lipid bilayer presents a major advantage over conventional continuum methods such as finite element or finite difference methods for cell membranes.
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Ho, D., B. Chu, H. Lee, K. Kuo, and C. D. Montemagno. "Fabrication of Hybrid Bionanodevices Based on Coupled Protein Functionality." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46012.

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Block copolymer-based membrane technology represents a versatile class of nanoscale materials in which biomolecules, such as membrane proteins, can be reconstituted. Among its many advantages over conventional lipid-based membrane systems, block copolymers can mimic natural cell biomembrane environments in a single chain, enabling large-area membrane fabrication using methods like Langmuir-Blodgett deposition, or spontaneous protein-functionalized nanovesicle formation. Based on this unique membrane property, a wide variety of membrane proteins possessing unique functionalities including pH/voltage gatable porosity, photon-activated proton pumping, and gradient-dependent production of electricity have been successfully inserted into these biomimetic systems.
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Zhang, Hao, Vishnu Baba Sundaresan, Sergio Salinas, and Robert Northcutt. "Electrochemical Analysis of Alamethicin Reconstituted Planar Bilayer Lipid Membranes Supported on Polypyrrole Membranes." In ASME 2011 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2011. http://dx.doi.org/10.1115/smasis2011-5038.

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Conducting polymers possess similarity in ion transport function to cell membranes and perform electro-chemo-mechanical energy conversion. In an in vitro setup, protein-reconstituted bilayer lipid membranes (bioderived membranes)perform similar energy conversion and behave like cell membranes. Inspired by the similarity in ionic function between a conducting polymer membrane and cell membrane, this article presents a thin-film laminated membrane in which alamethicin-reconstituted lipid bilayer membrane is supported on a polypyrrole membrane. Owing to the synthetic and bioderived nature of the components of the membrane, we refer to the laminated membrane as a hybrid bioderived membrane. In this article, we describe the fabrication steps and electrochemical characterization of the hybrid membrane. The fabrication steps include electropolymerization of pyrrole and vesicle fusion to result in a hybrid membrane; and the characterization involves electrical impedance spectroscopy, chronoamperometry and cyclic voltammetry. The resistance and capacitance of BLM have the magnitude of 4.6×109Ω-cm2 and 1.6×10−8 F/cm2.The conductance of alamethicin has the magnitude of 6.4×10−8 S/cm2. The change in ionic conductance of the bioderived membrane is due to the electrical field applied across alamethicin, a voltage-gated protein and produces a measurable change in the ionic concentration of the conducting polymer substrate.
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Zhu, Qiang, Zhangli Peng, and Robert J. Asaro. "Investigation of RBC Remodeling With a Multiscale Model." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13121.

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Erythrocyte (red blood cell, or RBC) possesses one of the simplest and best characterized molecular architectures among all cells. It contains cytosol enclosed inside a composite membrane consisting of a fluidic lipid bilayer reinforced by a single layer of protein skeleton pinned to it. In its normal state, this system demonstrates tremendous structural stability, manifested in its ability to sustain large dynamic deformations during circulation. On the other hand, it has been illustrated in experiments that triggered by mechanical loads structural remodeling may occur. A canonical example of this remodeling is vesiculation, referring to the partial separation of the lipid bilayer from the protein skeleton and the formation of vesicles that contain lipids only.
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Reports on the topic "Lipids Membrane proteins"

1

Sandermann, Heinrich, Duncan Jr., and Thomas M. Lipid-Dependent Membrane Enzymes. Kinetic Modelling of the Activation of Protein Kinase C by Phosphatidylserine. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302987.

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