"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
|
| MeSH Number(s) |
G02.111.570.820.709
|
| Concept/Terms |
Protein Conformation- Protein Conformation
- Conformation, Protein
- Conformations, Protein
- Protein Conformations
|
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 |
|---|
| 1993 | 2 | 8 | 10 |
| 1994 | 1 | 21 | 22 |
| 1995 | 1 | 10 | 11 |
| 1996 | 5 | 13 | 18 |
| 1997 | 5 | 8 | 13 |
| 1998 | 4 | 16 | 20 |
| 1999 | 1 | 18 | 19 |
| 2000 | 0 | 16 | 16 |
| 2001 | 0 | 15 | 15 |
| 2002 | 3 | 21 | 24 |
| 2003 | 1 | 26 | 27 |
| 2004 | 3 | 30 | 33 |
| 2005 | 2 | 30 | 32 |
| 2006 | 1 | 31 | 32 |
| 2007 | 5 | 24 | 29 |
| 2008 | 2 | 24 | 26 |
| 2009 | 3 | 24 | 27 |
| 2010 | 4 | 23 | 27 |
| 2011 | 4 | 18 | 22 |
| 2012 | 3 | 25 | 28 |
| 2013 | 5 | 14 | 19 |
| 2014 | 4 | 17 | 21 |
| 2015 | 2 | 22 | 24 |
| 2016 | 1 | 30 | 31 |
| 2017 | 1 | 14 | 15 |
| 2018 | 3 | 30 | 33 |
| 2019 | 4 | 13 | 17 |
| 2020 | 0 | 14 | 14 |
| 2021 | 2 | 15 | 17 |
| 2022 | 1 | 5 | 6 |
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Below are the most recent publications written about "Protein Conformation" by people in Profiles.
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Architecture of the cytoplasmic face of the nuclear pore. Science. 2022 06 10; 376(6598):eabm9129.
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Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition. Nat Commun. 2022 04 05; 13(1):1833.
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Challenges and Advantages of Accounting for Backbone Flexibility in Prediction of Protein-Protein Complexes. J Chem Theory Comput. 2022 Mar 08; 18(3):2016-2032.
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Intrinsically Disordered Proteins: Critical Components of the Wetware. Chem Rev. 2022 03 23; 122(6):6614-6633.
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Structural and functional insights into ABHD5, a ligand-regulated lipase co-activator. Sci Rep. 2022 02 16; 12(1):2565.
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Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein. Proc Natl Acad Sci U S A. 2022 01 04; 119(1).
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Prediction and Validation of a Protein's Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence. J Chem Theory Comput. 2022 Jan 11; 18(1):550-561.
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Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination. Nucleic Acids Res. 2021 12 16; 49(22):13135-13149.
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Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins. Proc Natl Acad Sci U S A. 2021 11 23; 118(47).
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Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell Rep. 2021 11 02; 37(5):109940.