 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 |
|---|
| 1980 | 0 | 2 | 2 | | 1981 | 1 | 1 | 2 | | 1982 | 0 | 1 | 1 | | 1984 | 0 | 2 | 2 | | 1985 | 0 | 2 | 2 | | 1986 | 0 | 3 | 3 | | 1987 | 0 | 2 | 2 | | 1988 | 0 | 1 | 1 | | 1989 | 0 | 3 | 3 | | 1990 | 0 | 6 | 6 | | 1991 | 1 | 5 | 6 | | 1992 | 1 | 5 | 6 | | 1993 | 0 | 1 | 1 | | 1994 | 1 | 4 | 5 | | 1995 | 3 | 4 | 7 | | 1996 | 0 | 7 | 7 | | 1997 | 4 | 5 | 9 | | 1998 | 1 | 10 | 11 | | 1999 | 1 | 8 | 9 | | 2000 | 0 | 8 | 8 | | 2001 | 0 | 9 | 9 | | 2002 | 0 | 9 | 9 | | 2003 | 0 | 9 | 9 | | 2004 | 1 | 10 | 11 | | 2005 | 0 | 13 | 13 | | 2006 | 1 | 9 | 10 | | 2007 | 0 | 3 | 3 | | 2008 | 0 | 6 | 6 | | 2009 | 0 | 8 | 8 | | 2010 | 2 | 5 | 7 | | 2011 | 1 | 4 | 5 | | 2012 | 2 | 5 | 7 | | 2013 | 2 | 14 | 16 | | 2014 | 0 | 6 | 6 | | 2015 | 0 | 10 | 10 | | 2016 | 0 | 12 | 12 | | 2017 | 0 | 6 | 6 | | 2018 | 0 | 8 | 8 | | 2019 | 1 | 4 | 5 | | 2020 | 0 | 9 | 9 | | 2021 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Conformation" by people in Profiles.
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Liu M, Das AK, Lincoff J, Sasmal S, Cheng SY, Vernon RM, Forman-Kay JD, Head-Gordon T. Configurational Entropy of Folded Proteins and Its Importance for Intrinsically Disordered Proteins. Int J Mol Sci. 2021 Mar 26; 22(7).
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Kucharska I, Thai E, Srivastava A, Rubinstein JL, Pomès R, Julien JP. Structural ordering of the Plasmodium berghei circumsporozoite protein repeats by inhibitory antibody 3D11. Elife. 2020 11 30; 9.
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Ripstein ZA, Vahidi S, Rubinstein JL, Kay LE. A pH-Dependent Conformational Switch Controls N. meningitidis ClpP Protease Function. J Am Chem Soc. 2020 12 09; 142(49):20519-20523.
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Jesin JA, Stone TA, Mitchell CJ, Reading E, Deber CM. Peptide-Based Approach to Inhibition of the Multidrug Resistance Efflux Pump AcrB. Biochemistry. 2020 10 20; 59(41):3973-3981.
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Conicella AE, Huang R, Ripstein ZA, Nguyen A, Wang E, Löhr T, Schuck P, Vendruscolo M, Rubinstein JL, Kay LE. An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase. Proc Natl Acad Sci U S A. 2020 10 20; 117(42):26226-26236.
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Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC. Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET. J Am Chem Soc. 2020 09 16; 142(37):15697-15710.
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Whitfield GB, Marmont LS, Bundalovic-Torma C, Razvi E, Roach EJ, Khursigara CM, Parkinson J, Howell PL. Discovery and characterization of a Gram-positive Pel polysaccharide biosynthetic gene cluster. PLoS Pathog. 2020 04; 16(4):e1008281.
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Vahidi S, Ripstein ZA, Juravsky JB, Rennella E, Goldberg AL, Mittermaier AK, Rubinstein JL, Kay LE. An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR. Proc Natl Acad Sci U S A. 2020 03 17; 117(11):5895-5906.
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Vasanthakumar T, Rubinstein JL. Structure and Roles of V-type ATPases. Trends Biochem Sci. 2020 04; 45(4):295-307.
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Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. Elife. 2020 01 09; 9.
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