 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 | 11 | 11 | | 1992 | 2 | 19 | 21 | | 1993 | 5 | 13 | 18 | | 1994 | 2 | 16 | 18 | | 1995 | 1 | 10 | 11 | | 1996 | 3 | 21 | 24 | | 1997 | 3 | 21 | 24 | | 1998 | 4 | 21 | 25 | | 1999 | 5 | 17 | 22 | | 2000 | 0 | 21 | 21 | | 2001 | 1 | 34 | 35 | | 2002 | 0 | 33 | 33 | | 2003 | 3 | 35 | 38 | | 2004 | 1 | 30 | 31 | | 2005 | 2 | 30 | 32 | | 2006 | 4 | 30 | 34 | | 2007 | 0 | 24 | 24 | | 2008 | 2 | 22 | 24 | | 2009 | 7 | 32 | 39 | | 2010 | 1 | 23 | 24 | | 2011 | 1 | 21 | 22 | | 2012 | 1 | 28 | 29 | | 2013 | 3 | 29 | 32 | | 2014 | 2 | 24 | 26 | | 2015 | 0 | 30 | 30 | | 2016 | 2 | 25 | 27 | | 2017 | 2 | 27 | 29 | | 2018 | 2 | 26 | 28 | | 2019 | 1 | 17 | 18 | | 2020 | 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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Sprenger KG, Louveau JE, Murugan PM, Chakraborty AK. Optimizing immunization protocols to elicit broadly neutralizing antibodies. Proc Natl Acad Sci U S A. 2020 08 18; 117(33):20077-20087.
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Rahman MM, Teng J, Worrell BT, Noviello CM, Lee M, Karlin A, Stowell MHB, Hibbs RE. Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Neuron. 2020 06 17; 106(6):952-962.e5.
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Vugmeyster L, Ostrovsky D, Fu R. Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-ß Fibrils. Chemphyschem. 2020 02 04; 21(3):220-231.
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Russo BC, Duncan JK, Wiscovitch AL, Hachey AC, Goldberg MB. Activation of Shigella flexneri type 3 secretion requires a host-induced conformational change to the translocon pore. PLoS Pathog. 2019 11; 15(11):e1007928.
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Baker SL, Munasinghe A, Kaupbayeva B, Rebecca Kang N, Certiat M, Murata H, Matyjaszewski K, Lin P, Colina CM, Russell AJ. Transforming protein-polymer conjugate purification by tuning protein solubility. Nat Commun. 2019 10 17; 10(1):4718.
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Vander Zanden CM, Wampler L, Bowers I, Watkins EB, Majewski J, Chi EY. Fibrillar and Nonfibrillar Amyloid Beta Structures Drive Two Modes of Membrane-Mediated Toxicity. Langmuir. 2019 12 03; 35(48):16024-16036.
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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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Maity K, Heumann JM, McGrath AP, Kopcho NJ, Hsu PK, Lee CW, Mapes JH, Garza D, Krishnan S, Morgan GP, Hendargo KJ, Klose T, Rees SD, Medrano-Soto A, Saier MH, Piñeros M, Komives EA, Schroeder JI, Chang G, Stowell MHB. Cryo-EM structure of OSCA1.2 from Oryza sativa elucidates the mechanical basis of potential membrane hyperosmolality gating. Proc Natl Acad Sci U S A. 2019 07 09; 116(28):14309-14318.
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Broniarczyk J, Massimi P, Pim D, Bergant Marušic M, Myers MP, Garcea RL, Banks L. Phosphorylation of Human Papillomavirus Type 16 L2 Contributes to Efficient Virus Infectious Entry. J Virol. 2019 07 01; 93(13).
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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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