Protein Structure, Secondary
"Protein Structure, Secondary" 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 level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Descriptor ID |
D017433
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MeSH Number(s) |
G02.111.570.820.709.600
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Concept/Terms |
Protein Structure, Secondary- Protein Structure, Secondary
- Secondary Protein Structure
- Protein Structures, Secondary
- Secondary Protein Structures
- Structure, Secondary Protein
- Structures, Secondary Protein
beta-Sheet Conformation, Protein- beta-Sheet Conformation, Protein
- Conformation, Protein beta-Sheet
- Conformations, Protein beta-Sheet
- Protein beta-Sheet Conformation
- Protein beta-Sheet Conformations
- beta Sheet Conformation, Protein
- beta-Sheet Conformations, Protein
- Protein Conformation, beta-Sheet
- Conformation, beta-Sheet Protein
- Conformations, beta-Sheet Protein
- Protein Conformation, beta Sheet
- Protein Conformations, beta-Sheet
- beta-Sheet Protein Conformation
- beta-Sheet Protein Conformations
Protein Conformation, beta-Strand- Protein Conformation, beta-Strand
- Conformation, beta-Strand Protein
- Conformations, beta-Strand Protein
- Protein Conformation, beta Strand
- Protein Conformations, beta-Strand
- beta-Strand Protein Conformation
- beta-Strand Protein Conformations
- beta-Strand Conformation, Protein
- Conformation, Protein beta-Strand
- Conformations, Protein beta-Strand
- Protein beta-Strand Conformation
- Protein beta-Strand Conformations
- beta Strand Conformation, Protein
- beta-Strand Conformations, Protein
alpha-Helical Conformation, Protein- alpha-Helical Conformation, Protein
- Conformation, Protein alpha-Helical
- Conformations, Protein alpha-Helical
- Protein alpha-Helical Conformation
- Protein alpha-Helical Conformations
- alpha Helical Conformation, Protein
- alpha-Helical Conformations, Protein
- Protein Conformation, alpha-Helical
- Conformation, alpha-Helical Protein
- Conformations, alpha-Helical Protein
- Protein Conformation, alpha Helical
- Protein Conformations, alpha-Helical
- alpha-Helical Protein Conformation
- alpha-Helical Protein Conformations
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Below are MeSH descriptors whose meaning is more general than "Protein Structure, Secondary".
Below are MeSH descriptors whose meaning is more specific than "Protein Structure, Secondary".
This graph shows the total number of publications written about "Protein Structure, Secondary" by people in this website by year, and whether "Protein Structure, Secondary" 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 |
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1996 | 1 | 0 | 1 | 1997 | 0 | 1 | 1 | 1998 | 0 | 1 | 1 | 1999 | 0 | 2 | 2 | 2000 | 0 | 2 | 2 | 2001 | 0 | 1 | 1 | 2002 | 0 | 2 | 2 | 2003 | 0 | 4 | 4 | 2004 | 0 | 3 | 3 | 2005 | 0 | 5 | 5 | 2006 | 0 | 3 | 3 | 2007 | 0 | 1 | 1 | 2008 | 0 | 1 | 1 | 2009 | 0 | 2 | 2 | 2011 | 0 | 3 | 3 | 2012 | 0 | 3 | 3 | 2013 | 0 | 2 | 2 | 2014 | 0 | 1 | 1 | 2015 | 0 | 1 | 1 | 2016 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein Structure, Secondary" by people in Profiles.
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Smith IN, Briggs JM. Structural mutation analysis of PTEN and its genotype-phenotype correlations in endometriosis and cancer. Proteins. 2016 Nov; 84(11):1625-1643.
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Paci M, Fox GE. Centers of motion associated with EF-Tu binding to the ribosome. RNA Biol. 2016 May 03; 13(5):524-30.
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Kim Y, Makowska-Grzyska M, Gorla SK, Gollapalli DR, Cuny GD, Joachimiak A, Hedstrom L. Structure of Cryptosporidium IMP dehydrogenase bound to an inhibitor with in vivo antiparasitic activity. Acta Crystallogr F Struct Biol Commun. 2015 May; 71(Pt 5):531-8.
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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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Craft JW, Zhang H, Charendoff MN, Mindrebo JT, Schwartz RJ, Briggs JM. Associations between the Rho kinase-1 catalytic and PH domain regulatory unit. J Mol Graph Model. 2013 Nov; 46:74-82.
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Charendoff MN, Shah HP, Briggs JM. New insights into the binding and catalytic mechanisms of Bacillus thuringiensis lactonase: insights into B. thuringiensis AiiA mechanism. PLoS One. 2013; 8(9):e75395.
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Ramesh B, Sendra VG, Cirino PC, Varadarajan N. Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins. J Biol Chem. 2012 Nov 09; 287(46):38580-9.
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Helsen CW, Glover JR. A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion. 2012 Jul 01; 6(3):234-9.
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Dong D, Wu B, Chow D, Hu M. Substrate selectivity of drug-metabolizing cytochrome P450s predicted from crystal structures and in silico modeling. Drug Metab Rev. 2012 May; 44(2):192-208.
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Zhu H, Briggs JM. Mechanistic role of NS4A and substrate in the activation of HCV NS3 protease. Proteins. 2011 Aug; 79(8):2428-43.
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