 Protein Denaturation
"Protein Denaturation" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
| Descriptor ID |
D011489
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| MeSH Number(s) |
E05.793.500 G01.154.651.750.500 G02.111.688.750.500
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| Concept/Terms |
Protein Denaturation- Protein Denaturation
- Denaturation, Protein
- Denaturations, Protein
- Protein Denaturations
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Below are MeSH descriptors whose meaning is more general than "Protein Denaturation".
Below are MeSH descriptors whose meaning is more specific than "Protein Denaturation".
This graph shows the total number of publications written about "Protein Denaturation" by people in this website by year, and whether "Protein Denaturation" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 | | 1996 | 0 | 3 | 3 | | 1998 | 0 | 2 | 2 | | 1999 | 1 | 2 | 3 | | 2000 | 0 | 2 | 2 | | 2001 | 0 | 1 | 1 | | 2002 | 0 | 6 | 6 | | 2003 | 0 | 4 | 4 | | 2004 | 0 | 1 | 1 | | 2005 | 0 | 3 | 3 | | 2006 | 1 | 0 | 1 | | 2007 | 0 | 2 | 2 | | 2008 | 0 | 4 | 4 | | 2009 | 0 | 2 | 2 | | 2010 | 1 | 2 | 3 | | 2011 | 0 | 1 | 1 | | 2012 | 0 | 1 | 1 | | 2013 | 0 | 1 | 1 | | 2014 | 0 | 4 | 4 | | 2015 | 1 | 1 | 2 | | 2017 | 0 | 2 | 2 | | 2019 | 0 | 2 | 2 | | 2020 | 0 | 1 | 1 | | 2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Denaturation" by people in Profiles.
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Becht DC, Leavens MJ, Zeng B, Rothfuss MT, Briknarov? K, Bowler BE. Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A. Biochemistry. 2022 05 03; 61(9):767-784.
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Nandi SK, Nahomi RB, Rankenberg J, Glomb MA, Nagaraj RH. Glycation-mediated inter-protein cross-linking is promoted by chaperone-client complexes of a-crystallin: Implications for lens aging and presbyopia. J Biol Chem. 2020 04 24; 295(17):5701-5716.
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Jacobson DR, Uyetake L, Perkins TT. Membrane-Protein Unfolding Intermediates Detected with Enhanced Precision Using a Zigzag Force Ramp. Biophys J. 2020 02 04; 118(3):667-675.
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Bull DS, Kienle DF, Chaparro Sosa AF, Nelson N, Roy S, Cha JN, Schwartz DK, Kaar JL, Goodwin AP. Surface-Templated Nanobubbles Protect Proteins from Surface-Mediated Denaturation. J Phys Chem Lett. 2019 Jun 06; 10(11):2641-2647.
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Stenzoski NE, Luan B, Holehouse AS, Raleigh DP. The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures. Biophys J. 2018 08 21; 115(4):655-663.
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Nagana Gowda GA, Djukovic D, Bettcher LF, Gu H, Raftery D. NMR-Guided Mass Spectrometry for Absolute Quantitation of Human Blood Metabolites. Anal Chem. 2018 02 06; 90(3):2001-2009.
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Danielson TA, Stine JM, Dar TA, Briknarova K, Bowler BE. Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c. Biochemistry. 2017 12 26; 56(51):6662-6676.
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Salmon L, Stull F, Sayle S, Cato C, Akg?l S, Foit L, Ahlstrom LS, Eisenmesser EZ, Al-Hashimi HM, Bardwell JCA, Horowitz S. The Mechanism of HdeA Unfolding and Chaperone Activation. J Mol Biol. 2018 01 05; 430(1):33-40.
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Lee S, Wang C, Liu H, Xiong J, Jiji R, Hong X, Yan X, Chen Z, Hammel M, Wang Y, Dai S, Wang J, Jiang C, Zhang G. Hydrogen bonds are a primary driving force for de novo protein folding. Acta Crystallogr D Struct Biol. 2017 Dec 01; 73(Pt 12):955-969.
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McClary WD, Sumida JP, Scian M, Pa?o L, Atkins WM. Membrane Fluidity Modulates Thermal Stability and Ligand Binding of Cytochrome P4503A4 in Lipid Nanodiscs. Biochemistry. 2016 Nov 15; 55(45):6258-6268.
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