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.
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
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 Harvard Catalyst Profiles by year, and whether "Protein Structure, Secondary" was a major or minor topic of these publication.
To see the data from this visualization as text,
click here.
Year | Major Topic | Minor Topic | Total |
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1994 | 11 | 22 | 33 |
1995 | 18 | 19 | 37 |
1996 | 6 | 17 | 23 |
1997 | 11 | 21 | 32 |
1998 | 12 | 28 | 40 |
1999 | 1 | 40 | 41 |
2000 | 1 | 38 | 39 |
2001 | 0 | 36 | 36 |
2002 | 1 | 30 | 31 |
2003 | 0 | 30 | 30 |
2004 | 0 | 32 | 32 |
2005 | 3 | 44 | 47 |
2006 | 3 | 43 | 46 |
2007 | 0 | 33 | 33 |
2008 | 2 | 39 | 41 |
2009 | 2 | 32 | 34 |
2010 | 2 | 40 | 42 |
2011 | 4 | 41 | 45 |
2012 | 0 | 45 | 45 |
2013 | 0 | 35 | 35 |
2014 | 0 | 42 | 42 |
2015 | 4 | 33 | 37 |
2016 | 0 | 30 | 30 |
2017 | 0 | 19 | 19 |
2018 | 1 | 22 | 23 |
2019 | 0 | 23 | 23 |
2020 | 0 | 14 | 14 |
2021 | 0 | 7 | 7 |
2022 | 0 | 2 | 2 |
2023 | 0 | 4 | 4 |
Below are the most recent publications written about "Protein Structure, Secondary" by people in Profiles.
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Constitutive activation and oncogenicity are mediated by loss of helical structure at the cytosolic boundary of thrombopoietin receptor mutant dimers. Elife. 2023 Jun 20; 12.
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A recombinant technique for mapping functional sites of heterotrimeric collagen helices: Collagen IV CB3 fragment as a prototype for integrin binding. J Biol Chem. 2023 07; 299(7):104901.
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Secondary structure of the human mitochondrial genome affects formation of deletions. BMC Biol. 2023 05 08; 21(1):103.
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Structure-based design of a SARS-CoV-2 Omicron-specific inhibitor. Proc Natl Acad Sci U S A. 2023 03 28; 120(13):e2300360120.
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RNA secondary structure packages evaluated and improved by high-throughput experiments. Nat Methods. 2022 10; 19(10):1234-1242.
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Molecular and structural basis of interactions of vitamin D3 hydroxyderivatives with aryl hydrocarbon receptor (AhR): An integrated experimental and computational study. Int J Biol Macromol. 2022 Jun 01; 209(Pt A):1111-1123.
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Structural basis for modulation of human NaV1.3 by clinical drug and selective antagonist. Nat Commun. 2022 03 11; 13(1):1286.
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Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site. Structure. 2022 02 03; 30(2):206-214.e4.
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Stapled ß-Hairpins Featuring 4-Mercaptoproline. J Am Chem Soc. 2021 09 22; 143(37):15039-15044.
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Membrane-Facilitated Receptor Access and Binding Mechanisms of Long-Acting ß2-Adrenergic Receptor Agonists. Mol Pharmacol. 2021 10; 100(4):406-427.