 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 |
|---|
| 1990 | 0 | 16 | 16 | | 1991 | 0 | 10 | 10 | | 1992 | 2 | 18 | 20 | | 1993 | 6 | 14 | 20 | | 1994 | 2 | 17 | 19 | | 1995 | 1 | 10 | 11 | | 1996 | 3 | 23 | 26 | | 1997 | 3 | 22 | 25 | | 1998 | 5 | 20 | 25 | | 1999 | 5 | 17 | 22 | | 2000 | 0 | 21 | 21 | | 2001 | 1 | 34 | 35 | | 2002 | 1 | 37 | 38 | | 2003 | 6 | 38 | 44 | | 2004 | 4 | 30 | 34 | | 2005 | 4 | 42 | 46 | | 2006 | 4 | 34 | 38 | | 2007 | 1 | 30 | 31 | | 2008 | 2 | 24 | 26 | | 2009 | 7 | 40 | 47 | | 2010 | 4 | 29 | 33 | | 2011 | 4 | 26 | 30 | | 2012 | 1 | 31 | 32 | | 2013 | 4 | 32 | 36 | | 2014 | 2 | 30 | 32 | | 2015 | 1 | 34 | 35 | | 2016 | 2 | 28 | 30 | | 2017 | 2 | 28 | 30 | | 2018 | 1 | 28 | 29 | | 2019 | 1 | 9 | 10 |
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Below are the most recent publications written about "Protein Conformation" by people in Profiles.
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Bayer KU, Schulman H. CaM Kinase: Still Inspiring at 40. Neuron. 2019 08 07; 103(3):380-394.
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Vugmeyster L, Au DF, Ostrovsky D, Fu R. Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-ß Fibrils. Chemphyschem. 2019 07 02; 20(13):1680-1689.
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Cao L, Yu B, Kong D, Cong Q, Yu T, Chen Z, Hu Z, Chang H, Zhong J, Baker D, He Y. Functional expression and characterization of the envelope glycoprotein E1E2 heterodimer of hepatitis C virus. PLoS Pathog. 2019 05; 15(5):e1007759.
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Boyken SE, Benhaim MA, Busch F, Jia M, Bick MJ, Choi H, Klima JC, Chen Z, Walkey C, Mileant A, Sahasrabuddhe A, Wei KY, Hodge EA, Byron S, Quijano-Rubio A, Sankaran B, King NP, Lippincott-Schwartz J, Wysocki VH, Lee KK, Baker D. De novo design of tunable, pH-driven conformational changes. Science. 2019 05 17; 364(6441):658-664.
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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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Pantouris G, Dioletis E, Chen Y, Thompson DC, Vasiliou V, Lolis EJ. Expression, purification and crystallization of the novel Xenopus tropicalis ALDH16B1, a homologue of human ALDH16A1. Chem Biol Interact. 2019 May 01; 304:168-172.
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Musselman CA, Kutateladze TG. Strategies for Generating Modified Nucleosomes: Applications within Structural Biology Studies. ACS Chem Biol. 2019 04 19; 14(4):579-586.
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Nandi SK, Rakete S, Nahomi RB, Michel C, Dunbar A, Fritz KS, Nagaraj RH. Succinylation Is a Gain-of-Function Modification in Human Lens aB-Crystallin. Biochemistry. 2019 03 05; 58(9):1260-1274.
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Leaton LA, Shortt J, Kichula KM, Tao S, Nemat-Gorgani N, Mentzer AJ, Oppenheimer SJ, Deng Z, Hollenbach JA, Gignoux CR, Guethlein LA, Parham P, Carrington M, Norman PJ. Conservation, Extensive Heterozygosity, and Convergence of Signaling Potential All Indicate a Critical Role for KIR3DL3 in Higher Primates. Front Immunol. 2019; 10:24.
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Jones DNM, Wang J, Murphy EJ. Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid. Biomol NMR Assign. 2019 04; 13(1):187-193.
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