"Protein Renaturation" 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.
The reconstitution of a protein's activity following denaturation.
| Descriptor ID |
D020673
|
| MeSH Number(s) |
G02.111.688.501.500
|
| Concept/Terms |
Protein Renaturation- Protein Renaturation
- Protein Renaturations
- Renaturations, Protein
- Renaturation, Protein
|
Below are MeSH descriptors whose meaning is more general than "Protein Renaturation".
Below are MeSH descriptors whose meaning is more specific than "Protein Renaturation".
This graph shows the total number of publications written about "Protein Renaturation" by people in this website by year, and whether "Protein Renaturation" was a major or minor topic of these publications.
To see the data from this visualization as text,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 0 | 1 | 1 |
| 2005 | 0 | 1 | 1 |
| 2008 | 1 | 0 | 1 |
| 2009 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Renaturation" by people in Profiles.
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Kent KP, Oltrogge LM, Boxer SG. Synthetic control of green fluorescent protein. J Am Chem Soc. 2009 Nov 11; 131(44):15988-9.
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Kathuria SV, Day IJ, Wallace LA, Matthews CR. Kinetic traps in the folding of beta alpha-repeat proteins: CheY initially misfolds before accessing the native conformation. J Mol Biol. 2008 Oct 03; 382(2):467-84.
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De M, Rotello VM. Synthetic "chaperones": nanoparticle-mediated refolding of thermally denatured proteins. Chem Commun (Camb). 2008 Aug 14; (30):3504-6.
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Arai M, Kondrashkina E, Kayatekin C, Matthews CR, Iwakura M, Bilsel O. Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein. J Mol Biol. 2007 Apr 20; 368(1):219-29.
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Wu Y, Vadrevu R, Kathuria S, Yang X, Matthews CR. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. J Mol Biol. 2007 Mar 09; 366(5):1624-38.
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Chow C, Kurt N, Murphy RM, Cavagnero S. Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution. Biophys J. 2006 Jan 01; 90(1):298-309.
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Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR. A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. J Mol Biol. 2002 Aug 02; 321(1):1-6.