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Relevant bibliographies by topics / Gramicidin channel and MJ0305 channel

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Academic literature on the topic 'Gramicidin channel and MJ0305 channel'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "Gramicidin channel and MJ0305 channel"

1

Koeppe, R. E., and O. S. Anderson. "Engineering the Gramicidin Channel." Annual Review of Biophysics and Biomolecular Structure 25, no. 1 (June 1996): 231–58. http://dx.doi.org/10.1146/annurev.bb.25.060196.001311.

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Etchebest, Catherine, and Alberte Pullman. "The gramicidin A channel." FEBS Letters 204, no. 2 (August 18, 1986): 261–65. http://dx.doi.org/10.1016/0014-5793(86)80824-9.

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Goulian, M., O. N. Mesquita, D. K. Fygenson, C. Nielsen, O. S. Andersen, and A. Libchaber. "Gramicidin Channel Kinetics under Tension." Biophysical Journal 74, no. 1 (January 1998): 328–37. http://dx.doi.org/10.1016/s0006-3495(98)77790-2.

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Roux, BenoÎt. "Computational Studies of the Gramicidin Channel." Accounts of Chemical Research 35, no. 6 (June 2002): 366–75. http://dx.doi.org/10.1021/ar010028v.

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Markham, Jeffrey C., Joseph A. Gowen, Timothy A. Cross, and David D. Busath. "Comparison of gramicidin A and gramicidin M channel conductance dispersities." Biochimica et Biophysica Acta (BBA) - Biomembranes 1513, no. 2 (August 2001): 185–92. http://dx.doi.org/10.1016/s0005-2736(01)00353-4.

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Koeppe, Roger E., Jean A. Paczkowski, and William L. Whaley. "Gramicidin K, a new linear channel-forming gramicidin from Bacillus brevis." Biochemistry 24, no. 12 (June 4, 1985): 2822–26. http://dx.doi.org/10.1021/bi00333a002.

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Nelson, Andrew. "Conducting Gramicidin Channel Activity in Phospholipid Monolayers." Biophysical Journal 80, no. 6 (June 2001): 2694–703. http://dx.doi.org/10.1016/s0006-3495(01)76238-8.

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Rostovtseva, Tatiana K., Horia I. Petrache, Namdar Kazemi, Elnaz Hassanzadeh, and Sergey M. Bezrukov. "Interfacial Polar Interactions Affect Gramicidin Channel Kinetics." Biophysical Journal 94, no. 4 (February 2008): L23—L25. http://dx.doi.org/10.1529/biophysj.107.120261.

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Pullman, A. "Energy profiles in the gramicidin A channel." Quarterly Reviews of Biophysics 20, no. 3-4 (November 1987): 173–200. http://dx.doi.org/10.1017/s0033583500004170.

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Gramicidin A (GA) is a linear pentadecapeptide made of alternating D and L residues, in which the N-and C-terminals are blocked by a formyl group (head) and an ethanolamine end (tail), respectively (Sarges & Witkop, 1964):

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Seoh, S. A., and D. Busath. "Gramicidin tryptophans mediate formamidinium-induced channel stabilization." Biophysical Journal 68, no. 6 (June 1995): 2271–79. http://dx.doi.org/10.1016/s0006-3495(95)80409-1.

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Dissertations / Theses on the topic "Gramicidin channel and MJ0305 channel"

1

Song, Hyun Deok. "Computer Simulation Studies of Ion Channels at High Temperatures." University of Cincinnati / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1328890332.

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Luk, Kai Yiu. "Statistical modeling and application of gramicidin A ion channel." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31984.

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Ion channels are aqueous pores in the cell membrane for selected ions to flow down their electrochemical gradient. These channels play a prominent role in a variety of biological processes in the human body. Determining the structure and function of ion channels is of fundamental importance in biology. Also, the selective conductivity and specific gating mechanism of ion channels have attracted much interest in the area of artificial molecular detectors. Ion channel based biosensors are developed to detect molecular species of interest in medical diagnostics, environmental monitoring and general bio-hazard detection. This thesis is concerned with statistical techniques used to describe ion channel permeation and to develop ion channel based biosensors. Brownian dynamics is a popular technique to simulate ion channel permeation but is too computationally expensive to run when ionic concentration is high. By fitting binding site statistics of BD simulation to a semi-Markov chain, we obtain a simpler model with conduction properties that are statistically the same as the simulations. This approach enables the use of extrapolation techniques to predict channel conduction when performing the actual simulation is computationally infeasible. Numerical studies on the simulation of gramicidin A channels are presented. In a separate study, we show the use of statistical modeling and detection techniques as part of a sensitive biosensing platform. A nano-scale biosensor is built by incorporating dimeric gramicidin A channels into bilayer membranes of giant unilamellar liposomes. The presence of specific target molecules changes the statistics of the biosensor's conduction. By capturing the change in real time, we devise a maximum likelihood detector to detect the presence of target molecules. The performance of the biosensor is tested with the addition of various target molecules known to inhibit conduction of gramicidin A channels. Experimental results show that the detection performed well even when the conductance change was difficult to visualize. The detection algorithm provides a sensitive detection system for ongoing development of membrane-based biosensors.
Applied Science, Faculty of
Electrical and Computer Engineering, Department of
Graduate

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Wang, Fang. "Peptide channel redesign: mutations of gramicidin A at membrane-water interface." Thesis, Boston College, 2012. http://hdl.handle.net/2345/3411.

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Thesis advisor: Jianmin Gao
My graduate research focuses on engineering and characterizing gramicidin A (gA), a natural fifteen-residue transmembrane channel peptide. It consists of D- and L- amino acids at alternate positions. gA is believed to fold into a β-helix in membranes, and two folded monomers at each leaflet of the lipid bilayer dimerize to form a transmembrane channel. gA shares the common features of other known membrane channels: a well defined structure that only allows the passage of specific ions, a gating mechanism, and a high abundance of aromatic residues. This dissertation includes two subprojects: I. Understanding Channel Formation: Aromatic Modifications of Gramicidin A Channel Ion channels are key elements in signaling and molecule transport, and therefore crucial for normal function of cells. Defective ion channels are known to be responsible for a number of diseases. Although hundreds of crystallographic structures of membrane proteins have been deposited into the PDB in the past few decades, our knowledge on this large family of proteins is still limited and mostly descriptive. Study of small peptides in model membranes is a good simplification of the more complex biological systems. In chapter 1, I will introduce my research using gA as a model system to understand the significant role of aromatic residues in membrane channel structure formation. Channel activities of these gA-Ar mutants were evaluated by ion leakage assays. The structure activity relationship of a library of gA mutants was discussed. The alternating chirality of amino acids was proven to be essential for gA channel activity. Several additional interesting observations are discussed. II. Towards Bacterium Specific Ion Channels: Solublized Gramicidin A as Potential Systemic Antibiotics The rapid development of multidrug resistance by pathogenic bacteria poses a serious threat to society and demands new antibiotics with different mechanisms. Often considered as a model transmembrane channel, gA also has proven antibiotic activities. The gA channel facilitates passive diffusion of water and monovalent cations (e.g. H+, Na+, K+) thus killing bacteria by disrupting the ion gradient across the cell membrane. However because of its poor solubility and high toxicity, its medicinal application as an antibiotic has been limited to topical reagents. A detailed understanding of gA allows rational optimization of the gA-WT to potential systemic antibiotics. Bacterial membranes are composed of a large fraction of anionic species, therefore, we hypothesize that strategic incorporation of cationic residues into gA will afford bacterium-specific toxicities. In addition, the charged residues will greatly improve the water solubility of gA. In chapter 2, I will introduce my research on developing soluble and bacterium specific gA as a potential systemic antibiotic. We firstly incorporated D-Lys at the C-terminus to obtain our first generation of gA based antibiotics. The best candidate (D-Leu10,12,14D-Lys gA) shows significantly increased water solubility (~ 1, 000 times) and therapeutic index (˃ 50 times). Modifications on the Lys side chain were then carried out to fine tune the antibiotic activities of these cationic gA. My research has pointed out a possible strategy to convert hydrophobic membrane channel peptides into potential systemic antibiotics. In addition to targeting the negative charges of bacterial membranes with cationic gA mutants, we proposed a novel strategy in which boronic acid is used to chase after the 1,2-diol substructure in the PG headgroup through boronate ester formation. Polyvalent display of boronic acids on a peptide scaffold results in enhanced binding with diols, showing promise of the boronate approach in the development of bacterium specific reagents
Thesis (PhD) — Boston College, 2012
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Chemistry

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Blake, Steven. "Designing nanosensors based on ion channel-forming derivatives of Gramicidin A." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3320124.

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Thesis (Ph. D.)--University of California, San Diego, 2008.
Title from first page of PDF file (viewed Sept. 11, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 111-121).

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Kubota, Shintaro. "Single Channel Analysis of Ion Transport across Membranes Containing Gramicidin A and KAT1 Channels." Kyoto University, 2016. http://hdl.handle.net/2433/215593.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第19767号
農博第2163号
新制||農||1040(附属図書館)
学位論文||H28||N4983(農学部図書室)
32803
京都大学大学院農学研究科応用生命科学専攻
(主査)教授加納健司, 教授三芳秀人, 教授三上文三
学位規則第4条第1項該当

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WANG, ZHENG. "HIERARCHICAL APPROACH TO PREDICTING TRANSPORT PROPERTIES OF A GRAMICIDIN ION CHANNEL WITHIN A LIPID BILAYER." University of Cincinnati / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1069794237.

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Stephens, Brian Dominic. "BIOCOMPOSITE PROTON EXCHANGE MEMBRANES*." University of Cincinnati / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1147968573.

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Herasymova, Nataliya. "Gramicidin A and cyclic peptides channel conductances in black lipid membranes." 2010. http://hdl.handle.net/10090/15143.

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Olah, Glenn Allen. "Thallium ion distribution in the gramicidin ion conducting channel determined by x-ray diffraction." Thesis, 1990. http://hdl.handle.net/1911/16378.

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Gramicidin is the best characterized transmembrane ion channel. An opulence of biochemical and physiological data exists and it is the only channel for which a relatively well-defined structure is known. Thus, it has been proven to be an ideal model for actual physiological channels by providing valuable insight into a channel's structural/functional properties. Although much is known about the gramicidin channel, there is still no solid experimental data on the channel molecular dimensions. Therefore, this thesis supplies a very crucial piece of experimental structural data; namely, the direct location of two symmetric cation binding sites within the channel by x-ray diffraction. The binding sites are located at 9.4 $\pm$ 0.4 A about the midpoint of the channel. A previous $\sp{13}$C NMR study (Urry et al., 1982a,b; Urry, 1983) pinpointed cation binding between Trp-11 and Trp-13, and, based on rigid molecular models, this puts the binding sites at 11.0-11.5 A, which is at least 1.2 A larger than the value reported here. This suggests a considerable plasticity of the gramicidin channel consistent with conclusions drawn from recent molecular dynamic simulations (Roux and Karplus, 1988). Also, the smaller value leads to an elegant qualitative picture in which the flexible ends of the channel can conveniently provide the gating mechanism that transmits cations and blocks anions.

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CAI, WEI-HONG, and 蔡煒鴻. "The effect of EM field on the motion of Na﹢ through the gramicidin a ion channel." Thesis, 1993. http://ndltd.ncl.edu.tw/handle/56555049119180521010.

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Books on the topic "Gramicidin channel and MJ0305 channel"

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Chadwick, Derek J., and Gail Cardew, eds. Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides. Chichester, UK: John Wiley & Sons, Ltd., 1999. http://dx.doi.org/10.1002/9780470515716.

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Cardew, Gail, and Derek J. Chadwick. Gramicidin and Related Ion Channel-Forming Peptides. Wiley & Sons, Incorporated, John, 2008.

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3

Derek, Chadwick, Cardew Gail, Novartis Foundation, and Symposium on Gramicidin and Related Ion Channel-forming Peptides (1998 : London, England), eds. Gramicidin and related ion channel-forming peptides. Chichester: Wiley, 1999.

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Gail, Cardew, Chadwick Derek, Novartis Foundation, and Symposium on Gramicidin and Related Ion Channel-forming Peptides (1998 : London, England), eds. Gramicidin and related ion channel-forming peptides. Chichester: Wiley, 1999.

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Symposium, Novartis Foundation. Gramicidin and Related Ion Channel-Forming Peptides - No. 225. John Wiley & Sons, 1999.

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Book chapters on the topic "Gramicidin channel and MJ0305 channel"

1

Wallace, B. A. "Introduction: Gramicidin, a Model Ion Channel." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 1–3. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch1.

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Etchebest, Catherine, and Alberte Pullman. "The Gramicidin a Channel: Left Versus Right-Handed Helix." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 167–85. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-3075-9_12.

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3

Busath, David, Greg Hemsley, Terry Bridal, Michael Pear, Kevin Gaffney, and Martin Karplus. "Guanidinium as a Probe of the Gramicidin Channel Interior." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 187–201. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-3075-9_13.

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4

Urry, Dan W. "On the Molecular Structure of the Gramicidin Transmembrane Channel." In The Enzymes of Biological Membranes, 229–57. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4598-5_6.

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Fairbanks, Teresa G., Chris L. Andrus, and David D. Busath. "Lorentzian Noise in Single Gramicidin A Channel Formamidinium Currents." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 74–92. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch6.

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Roux, Benoît, and Thomas B. Woolf. "The Binding Site of Sodium in the Gramicidin A Channel." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 113–27. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch8.

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Cornell, B. A., V. L. B. Braach-Maksvytis, L. G. King, P. D. J. Osman, B. Raguse, L. Wieczorek, and R. J. Pace. "The Gramicidin-Based Biosensor: A Functioning Nano-Machine." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 231–59. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch15.

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Reinhardt, R., K. Janko, and E. Bamberg. "Single Channel Conductance Changes of the Desethanolamine-Gramicidin Through pH Variations." In Electrical Double Layers in Biology, 91–102. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-8145-7_7.

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Wallace, B. A. "Summary: What We have Learned about Gramicidin and Other Ion Channels." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 260–62. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch16.

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Koeppe, Roger E., Denise V. Greathouse, Lyndon L. Providence, S. Shobana, and Olaf S. Andersen. "Design and Characterization of Gramicidin Channels with Side Chain or Backbone Mutations." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 44–61. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch4.

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Conference papers on the topic "Gramicidin channel and MJ0305 channel"

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Krishnamurthy, Vikram, Kai Yiu Luk, Bruce Cornell, and Don Martin. "Real-Time Molecular Detectors using Gramicidin Ion Channel Nano-Biosensors." In 2007 IEEE International Conference on Acoustics, Speech and Signal Processing - ICASSP '07. IEEE, 2007. http://dx.doi.org/10.1109/icassp.2007.366701.

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Esquembre, Rocío, José Antonio Poveda, Ricardo Mallavia, and C. Reyes Mateo. "Immobilization and characterization of the transmembrane ion channel peptide gramicidin in a sol-gel matrix." In Microtechnologies for the New Millennium, edited by Paolo Arena, Ángel Rodríguez-Vázquez, and Gustavo Liñán-Cembrano. SPIE, 2007. http://dx.doi.org/10.1117/12.721676.

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Shao, C., M. Colombini, and D. L. DeVoe. "Planar Phospholipid Membrane Formation in Open Well Thermoplastic Chips." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-11432.

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A key requirement for the effective study of interactions between analytes and ion channels is the ability to dynamically vary analyte type and concentration to a membrane-bound ion channel within a planar phospholipid membrane (PPM). Here an open well microfluidic PPM apparatus supporting dynamic perfusion is presented. The plastic chip supports the manual formation of bilayer membranes that are resistant to pressure disturbances during perfusion with stability on the order of several hours. Using a chamber volume of 20 μL and a flow rate of 0.5 μL/min, the system enables rapid perfusion without breaking the membrane. The perfusion capability is demonstrated through gramicidin ion channel measurements.

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