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Relevant bibliographies by topics / Protein unfolding

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Academic literature on the topic 'Protein unfolding'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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Journal articles on the topic "Protein unfolding"

1

Finkelstein, A. V. "Can protein unfolding simulate protein folding?" Protein Engineering Design and Selection 10, no. 8 (1997): 843–45. http://dx.doi.org/10.1093/protein/10.8.843.

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Toofanny, Rudesh D., Sara Calhoun, Amanda L. Jonsson та Valerie Daggett. "Shared unfolding pathways of unrelated immunoglobulin-like β-sandwich proteins". Protein Engineering, Design and Selection 32, № 7 (2019): 331–45. http://dx.doi.org/10.1093/protein/gzz040.

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Abstract The Dynameomics project contains native state and unfolding simulations of 807 protein domains, where each domain is representative of a different metafold; these metafolds encompass ~97% of protein fold space. There is a long-standing question in structural biology as to whether proteins in the same fold family share the same folding/unfolding characteristics. Using molecular dynamics simulations from the Dynameomics project, we conducted a detailed study of protein unfolding/folding pathways for 5 protein domains from the immunoglobulin (Ig)-like β-sandwich metafold (the highest ran

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3

Seelig, Joachim, and Anna Seelig. "Protein Unfolding—Thermodynamic Perspectives and Unfolding Models." International Journal of Molecular Sciences 24, no. 6 (2023): 5457. http://dx.doi.org/10.3390/ijms24065457.

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We review the key steps leading to an improved analysis of thermal protein unfolding. Thermal unfolding is a dynamic cooperative process with many short-lived intermediates. Protein unfolding has been measured by various spectroscopic techniques that reveal structural changes, and by differential scanning calorimetry (DSC) that provides the heat capacity change Cp(T). The corresponding temperature profiles of enthalpy ΔH(T), entropy ΔS(T), and free energy ΔG(T) have thus far been evaluated using a chemical equilibrium two-state model. Taking a different approach, we demonstrated that the tempe

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Itkonen, Jaakko, Leo Ghemtio, Daniela Pellegrino, Pia J. Jokela (née Heinonen), Henri Xhaard, and Marco G. Casteleijn. "Analysis of Biologics Molecular Descriptors towards Predictive Modelling for Protein Drug Development Using Time-Gated Raman Spectroscopy." Pharmaceutics 14, no. 8 (2022): 1639. http://dx.doi.org/10.3390/pharmaceutics14081639.

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Pharmaceutical proteins, compared to small molecular weight drugs, are relatively fragile molecules, thus necessitating monitoring protein unfolding and aggregation during production and post-marketing. Currently, many analytical techniques take offline measurements, which cannot directly assess protein folding during production and unfolding during processing and storage. In addition, several orthogonal techniques are needed during production and market surveillance. In this study, we introduce the use of time-gated Raman spectroscopy to identify molecular descriptors of protein unfolding. Ra

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Creighton, T. E. "Unfolding protein folding." Nature 352, no. 6330 (1991): 17–18. http://dx.doi.org/10.1038/352017a0.

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Glyakina, Anna, and Oxana Galzitskaya. "How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?" Biomolecules 10, no. 2 (2020): 197. http://dx.doi.org/10.3390/biom10020197.

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The correlations between the logarithm of the unfolding rate of 108 proteins and their structural parameters were calculated. We showed that there is a good correlation between the logarithm of folding rates (in native conditions) and unfolding rates (in denaturing conditions) (0.79) and protein stability and unfolding rate (0.79). Thus, the faster the protein folds, the faster it unfolds. Folding and unfolding rates are higher for the proteins with two-state kinetics, in comparison with the proteins with multi-state kinetics. At the same time, two-state bacterial proteins folds and unfolds tw

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Oepen, Kristin, Veronika Mater, and Dirk Schneider. "Unfolding Individual Domains of BmrA, a Bacterial ABC Transporter Involved in Multidrug Resistance." International Journal of Molecular Sciences 24, no. 6 (2023): 5239. http://dx.doi.org/10.3390/ijms24065239.

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The folding and stability of proteins are often studied via unfolding (and refolding) a protein with urea. Yet, in the case of membrane integral protein domains, which are shielded by a membrane or a membrane mimetic, urea generally does not induce unfolding. However, the unfolding of α-helical membrane proteins may be induced by the addition of sodium dodecyl sulfate (SDS). When protein unfolding is followed via monitoring changes in Trp fluorescence characteristics, the contributions of individual Trp residues often cannot be disentangled, and, consequently, the folding and stability of the

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Hartl, F. Ulrich. "Unfolding the chaperone story." Molecular Biology of the Cell 28, no. 22 (2017): 2919–23. http://dx.doi.org/10.1091/mbc.e17-07-0480.

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Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen’s discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the

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Torres-Sánchez, Alejandro, Juan M. Vanegas, Prashant K. Purohit, and Marino Arroyo. "Combined molecular/continuum modeling reveals the role of friction during fast unfolding of coiled-coil proteins." Soft Matter 15, no. 24 (2019): 4961–75. http://dx.doi.org/10.1039/c9sm00117d.

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Coiled-coils are filamentous proteins capable of reversible unfolding. We show that hydrodynamic interactions with the solvent, usually neglected in theories of protein unfolding, are critical to understand their unfolding at high rates.

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Dubois, Cécile, Vicente J. Planelles-Herrero, Camille Tillatte-Tripodi та ін. "Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1". International Journal of Molecular Sciences 22, № 7 (2021): 3597. http://dx.doi.org/10.3390/ijms22073597.

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When combined with NMR spectroscopy, high hydrostatic pressure is an alternative perturbation method used to destabilize globular proteins that has proven to be particularly well suited for exploring the unfolding energy landscape of small single-domain proteins. To date, investigations of the unfolding landscape of all-β or mixed-α/β protein scaffolds are well documented, whereas such data are lacking for all-α protein domains. Here we report the NMR study of the unfolding pathways of GIPC1-GH2, a small α-helical bundle domain made of four antiparallel α-helices. High-pressure perturbation wa

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Dissertations / Theses on the topic "Protein unfolding"

1

Moraitakis, George. "Protein unfolding and disease." Thesis, Birkbeck (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.272112.

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Causton, Edward William Thomas. "Protein mechanical unfolding in multiple dimensions." Thesis, University of Leeds, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.535690.

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Jakus-Pol, Joanna Ewa. "Pressure perturbation calorimetry of protein unfolding." Thesis, University of Glasgow, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.412944.

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Sadler, David Paul. "Mechanically unfolding variants of protein L." Thesis, University of Leeds, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.444035.

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Krammer, André Thomas. "Computational studies of protein-membrane interactions and forced unfolding of proteins /." Thesis, Connect to this title online; UW restricted, 2000. http://hdl.handle.net/1773/9697.

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Zinober-Moore, Rebecca C. "Elasticity and mechanical unfolding of globular protein domains." Thesis, University of Leeds, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426849.

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Saladino, G. "FREE ENERGIES IN BIOMOLECULAR SIMULATIONS: FROM PROTEIN-PROTEIN INTERACTIONS TO UNFOLDING INHIBITION." Doctoral thesis, Università degli Studi di Milano, 2010. http://hdl.handle.net/2434/150127.

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Part I - Microtubules are polymeric structures formed by the self association of tubulin dimers. They are extremely dynamical structures, that can undergo phases of growing and shrinking, playing a key role during cells proliferation process. Due to its importance for mitosis, tubulin is the target of many anticancer drugs currently in use or under clinical trial. The success of these molecules, however, is limited by the onset of resistant tumor cells during the treatment, so new resistance-proof compounds need to be developed. We analyze the protein-protein interactions allowing microt

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Berry, Yoke. "The effect of pulsed electromagnetic fields on protein unfolding." Access electronically, 2005. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20060713.142625/index.html.

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Knaggs, Michael Henry. "Protein unfolding and stability : a computational study of barnase." Thesis, Birkbeck (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325104.

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Miriani, M. "PROTEIN UNFOLDING ON INTERFACES: A STRUCTURAL AND FUNCTIONAL STUDY." Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/170496.

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The spontaneous adsorption of protein molecules on interfaces is an ubiquitous phenomenon in natural and man-made systems. The structural rearrangement caused by the direct contact with the sorbent phase may affect protein biological activity, including bioavailability, and ability to bind micro- and macromolecular ligands. Moreover, protein immunoreactivity has been assessed to change if protein molecules interact with an hydrophobic phase; indeed adjuvant are hydrophobic substances that act as enhancers in antibodies production. Whether proteins unfold randomly or through subsequent ordered

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Books on the topic "Protein unfolding"

1

Sadana, Ajit. Bioseparation of proteins: Unfolding/folding and validations. Academic Press, 1998.

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2

Feldmann, Richard J. Understanding protein architecture through simulated unfolding. Division of Computer Research and Technology, National Institutes of Health, 1986.

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3

Wako, Hiroshi. Folding/unfolding kinetics of lattice proteins by applying a simple statistical mechanical model for protein folding. Nova Biomedical, 2011.

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Wako, Hiroshi. Folding/unfolding kinetics of lattice proteins by applying a simple statistical mechanical model for protein folding. Nova Biomedical, 2011.

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5

Kuo, Tzu-Ling. Probing static disorder in protein unfolding and chemical reactions by single-molecule force spectroscopy. [publisher not identified], 2011.

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6

Li, Zhiying. Simulated force-induced stretching of protein a[alpha}-helices: The effect of primary sequence on the unfolding mechanism. Laurentian University, School of Graduate Studies, 2004.

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7

Sherwood, Dennis, and Paul Dalby. Macromolecular conformations and interactions. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.003.0025.

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As a polymer of many amino acids, any given protein can, in principle, adopt a huge number of configurations. In reality, however, the biologically stable protein adopts a single configuration that is stable over time. Thermodynamically, this configuration must represent a Gibbs free energy minimum. This chapter therefore explores how the thermodynamics and kinetics of protein folding and unfolding can be investigated experimentally (using, for example, chaotropes, heating or ligand interactions), and how these measurements can be used to enrich our understanding of protein configurations and

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8

Sadana, Ajit, and Satinder Ahuja. Bioseparations of Proteins: Unfolding/Folding and Validations. Elsevier Science & Technology Books, 1997.

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9

Castello, Ignasi Velazquez I. Proteins in Vacuo Molecular Dynamics Studies of Hen Egg White Lysozyme Submitted to Unfolding and Relaxation Conditions. Uppsala Universitet, 1999.

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Volpi, Frédéric. Introduction. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190642921.003.0001.

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The chapter considers two ways of conceptualizing the events of the Arab uprisings. These transformations can be explained by actor-centric narratives stressing the contingency of protest episodes and of their outcomes. They can also be portrayed as the unfolding of longer-term trends in which specific combinations of economic, military, social and political factors repeatedly shape the form and outcomes of change. The chapter highlights the importance of meaning-making in the construction of the causality of the 2011 uprisings in North Africa. It points to the centrality of interpretation in

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Book chapters on the topic "Protein unfolding"

1

Garcia, Angel E. "Atomistic Simulations of Thermal Unfolding." In Protein Folding. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1716-8_18.

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Gruia, Andreea Daniela, Stefan Fischer, and Jeremy C. Smith. "Computer Simulation of Protein Unfolding." In High Performance Computing in Science and Engineering ’01. Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56034-7_25.

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Wetzel, Ronald, L. Jeanne Perry, Michael G. Mulkerrin, and L. Michael Randall. "Unfolding and Inactivation." In Protein Design and the Development of New Therapeutics and Vaccines. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5739-1_5.

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4

De Sancho, David, and Victor Muñoz. "Prediction of Folding and Unfolding Rates of Proteins with Simple Models." In Protein Folding. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1716-8_20.

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5

Jiang, Hou-Li, Bo Jiang, Zhan-Jun Song, Zhen-Hua Deng, Song-Cheng Yang, and De-Xu Zhu. "Protein unfolding studied by FTIR spectroscopy." In Peptides. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-010-9069-8_25.

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Mattoo, Rayees U. H., and Pierre Goloubinoff. "Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins." In Protein Aggregation in Bacteria. John Wiley & Sons, Inc., 2014. http://dx.doi.org/10.1002/9781118845363.ch2.

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Li, Pan T. X., and Ignacio Tinoco. "Thermodynamics and Kinetics of RNA Unfolding and Refolding." In Non-Protein Coding RNAs. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-70840-7_3.

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Pfanner, Nikolaus. "Mitochondrial Protein Import: Unfolding and Refolding of Precursor Proteins." In Stress Proteins. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75815-7_6.

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Malhotra, Pooja, and Jayant B. Udgaonkar. "Native State Hydrogen Exchange-Mass Spectrometry Methods to Probe Protein Folding and Unfolding." In Protein Folding. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1716-8_8.

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Schillinger, Jasmin, and Doris Hellerschmied. "Targeted Protein Unfolding at the Golgi Apparatus." In Methods in Molecular Biology. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2639-9_39.

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Conference papers on the topic "Protein unfolding"

1

Basha, Shaik, Shanmukha Sreeya Devarakonda, Darshan Chikkanayakanahalli Mukunda, et al. "Investigation of Protein Thermal Aggregation Using Autofluorescence Spectroscopy." In Frontiers in Optics. Optica Publishing Group, 2024. https://doi.org/10.1364/fio.2024.jd4a.6.

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Yu, Meng, Wei Si, and Jingjie Sha. "Molecular Dynamics Simulation for Protein Unfolding." In 2020 IEEE 15th International Conference on Nano/Micro Engineered and Molecular System (NEMS). IEEE, 2020. http://dx.doi.org/10.1109/nems50311.2020.9265552.

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Yuan, Runyi, and Wei Si. "Protein Unfolding with MoS2/SnS2 Heterostructure." In 2022 IEEE International Conference on Manipulation, Manufacturing and Measurement on the Nanoscale (3M-NANO). IEEE, 2022. http://dx.doi.org/10.1109/3m-nano56083.2022.9941518.

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Purohit, Prashant K. "Fibrin Networks Sustain Large Extensions Due to Unfolding Proteins." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13125.

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Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We show how these networks give rise to the remarkable extensibility and elasticity of blood clots by determining structural and mechanical properties of the clot at the network, fiber, and molecular levels. The force required to stretch a clot initially rises almost linearly and is accompanied by a dramatic decrease in the clot volume. These macroscopic changes are accompanied by fiber alignment and bundling following forced protein unfolding. We develop constitutive models to integrate observat

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Yang, Jingqi, and Lingyun Chen. "Effects of extraction methods on the composition, structure, and gelling mechanism of pea proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/yyzj7229.

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A a systematic understanding of pea protein composition, conformation and functionalities as impacted by extraction methods is limited. Moreover, previous works focused on investigating the effects of gelling conditions on gel properties and showed that pea protein had significantly lower gelling capacity and weaker gel texture than soy proteins. However, gelling mechanism of pea protein has not been fully understood yet. Six protein isolation methods were selected, including air-classification (AC), alkaline extraction followed by isoelectric precipitation (AI) or ultrafiltration (AU), salt s

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Stahl, F., D. Berrar, C. Silva, R. J. Rodrigues, R. M. M. Brito, and W. Dubitzky. "Grid warehousing of molecular dynamics protein unfolding data." In CCGrid 2005. IEEE International Symposium on Cluster Computing and the Grid, 2005. IEEE, 2005. http://dx.doi.org/10.1109/ccgrid.2005.1558594.

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Silva, Candida G., Vitaliy Ostropytskyy, Nuno Loureiro-Ferreira, et al. "P-found: The Protein Folding and Unfolding Simulation Repository." In 2006 IEEE Symposium on Computational Intelligence and Bioinformatics and Computational Biology. IEEE, 2006. http://dx.doi.org/10.1109/cibcb.2006.330978.

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Sumit, Sugam Kumar, and V. K. Aswal. "Role of electrostatic interaction on surfactant induced protein unfolding." In SOLID STATE PHYSICS: PROCEEDINGS OF THE 57TH DAE SOLID STATE PHYSICS SYMPOSIUM 2012. AIP, 2013. http://dx.doi.org/10.1063/1.4790960.

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Ferreira, P. G., C. G. Silva, R. M. M. Brito, and P. J. Azevedo. "A Closer Look on Protein Unfolding Simulations through Hierarchical Clustering." In 2007 4th Symposium on Computational Intelligence in Bioinformatics and Computational Biology. IEEE, 2007. http://dx.doi.org/10.1109/cibcb.2007.4221256.

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Watson, Gregory S., Jolanta A. Watson, Christopher L. Brown, and Sverre Myhra. "Protein folding and unfolding by force microscopy: a novel inverse methodology." In Smart Materials, Nano-, and Micro-Smart Systems, edited by Jung-Chih Chiao, David N. Jamieson, Lorenzo Faraone, and Andrew S. Dzurak. SPIE, 2005. http://dx.doi.org/10.1117/12.582646.

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Reports on the topic "Protein unfolding"

1

Walsh, Alex. The Contentious Politics of Tunisia’s Natural Resource Management and the Prospects of the Renewable Energy Transition. Institute of Development Studies (IDS), 2021. http://dx.doi.org/10.19088/k4d.2021.048.

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For many decades in Tunisia, there has been a robust link between natural resource management and contentious national and local politics. These disputes manifest in the form of protests, sit-ins, the disruption of production and distribution and legal suits on the one hand, and corporate and government response using coercive and concessionary measures on the other. Residents of resource-rich areas and their allies protest the inequitable distribution of their local natural wealth and the degradation of their health, land, water, soil and air. They contest a dynamic that tends to bring greate

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