 Protein Conformation
"Protein Conformation" 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 characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
| Descriptor ID |
D011487
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| MeSH Number(s) |
G02.111.570.820.709
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| Concept/Terms |
Protein Conformation- Protein Conformation
- Conformation, Protein
- Conformations, Protein
- Protein Conformations
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Below are MeSH descriptors whose meaning is more general than "Protein Conformation".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation".
This graph shows the total number of publications written about "Protein Conformation" by people in this website by year, and whether "Protein Conformation" 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 |
|---|
| 1984 | 0 | 1 | 1 | | 1986 | 0 | 1 | 1 | | 1989 | 1 | 1 | 2 | | 1992 | 0 | 1 | 1 | | 1994 | 0 | 1 | 1 | | 1995 | 1 | 3 | 4 | | 1996 | 1 | 1 | 2 | | 1997 | 0 | 3 | 3 | | 1998 | 0 | 2 | 2 | | 1999 | 0 | 3 | 3 | | 2000 | 0 | 3 | 3 | | 2001 | 1 | 6 | 7 | | 2002 | 0 | 10 | 10 | | 2003 | 0 | 9 | 9 | | 2004 | 1 | 7 | 8 | | 2005 | 0 | 8 | 8 | | 2006 | 1 | 3 | 4 | | 2007 | 0 | 6 | 6 | | 2008 | 1 | 7 | 8 | | 2009 | 1 | 8 | 9 | | 2010 | 1 | 1 | 2 | | 2011 | 0 | 3 | 3 | | 2012 | 0 | 3 | 3 | | 2013 | 1 | 3 | 4 | | 2014 | 0 | 3 | 3 | | 2015 | 0 | 3 | 3 |
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Below are the most recent publications written about "Protein Conformation" by people in Profiles.
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Vorontsova MA, Maes D, Vekilov PG. Recent advances in the understanding of two-step nucleation of protein crystals. Faraday Discuss. 2015; 179:27-40.
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Gherbi K, May LT, Baker JG, Briddon SJ, Hill SJ. Negative cooperativity across ß1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ß1-adrenoceptor binding conformation. FASEB J. 2015 Jul; 29(7):2859-71.
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Brader ML, Estey T, Bai S, Alston RW, Lucas KK, Lantz S, Landsman P, Maloney KM. Examination of thermal unfolding and aggregation profiles of a series of developable therapeutic monoclonal antibodies. Mol Pharm. 2015 Apr 06; 12(4):1005-17.
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Craft JW, Shen TW, Brier LM, Briggs JM. Biophysical characteristics of cholera toxin and Escherichia coli heat-labile enterotoxin structure and chemistry lead to differential toxicity. J Phys Chem B. 2015 Jan 22; 119(3):1048-61.
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Li Y, Cirino PC. Recent advances in engineering proteins for biocatalysis. Biotechnol Bioeng. 2014 Jul; 111(7):1273-87.
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Baker JG, Proudman RG, Hill SJ. Identification of key residues in transmembrane 4 responsible for the secondary, low-affinity conformation of the human ß1-adrenoceptor. Mol Pharmacol. 2014 May; 85(5):811-29.
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Baker JG, Proudman RG, Hill SJ. Impact of polymorphic variants on the molecular pharmacology of the two-agonist conformations of the human ß1-adrenoceptor. PLoS One. 2013; 8(11):e77582.
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Oliveira GS, Leite FL, Amarante AM, Franca EF, Cunha RA, Briggs JM, Freitas LC. Molecular modeling of enzyme attachment on AFM probes. J Mol Graph Model. 2013 Sep; 45:128-36.
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Liu M, Bender SA, Cuny GD, Sherman W, Glicksman M, Ray SS. Type II kinase inhibitors show an unexpected inhibition mode against Parkinson's disease-linked LRRK2 mutant G2019S. Biochemistry. 2013 Mar 12; 52(10):1725-36.
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Baranovic J, Ramanujan CS, Kasai N, Midgett CR, Madden DR, Torimitsu K, Ryan JF. Reconstitution of homomeric GluA2(flop) receptors in supported lipid membranes: functional and structural properties. J Biol Chem. 2013 Mar 22; 288(12):8647-57.
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