Protein Conformation, alpha-Helical
"Protein Conformation, alpha-Helical" 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.
A secondary structure of proteins that is a right-handed helix or coil, where each amino (N-H) group of the peptide backbone contributes a hydrogen bond to the carbonyl(C=O) group of the amino acid four residues N-terminal to it (n-4). It is the most common type of secondary structure.
| Descriptor ID |
D000072756
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| MeSH Number(s) |
G02.111.570.820.709.600.020
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| Concept/Terms |
Protein Conformation, alpha-Helical- Protein Conformation, alpha-Helical
- Protein Conformation, alpha Helical
- alpha-Helices
- alpha Helices
- alpha-Helical Conformation, Protein
- Conformation, Protein alpha-Helical
- Conformations, Protein alpha-Helical
- alpha Helical Conformation, Protein
- alpha-Helical Conformations, Protein
- alpha-Helical Protein Conformation
- Conformation, alpha-Helical Protein
- Conformations, alpha-Helical Protein
- Protein Conformations, alpha-Helical
- alpha Helical Protein Conformation
- alpha-Helical Protein Conformations
- alpha-Helix
- alpha Helix
- alpha-Helical Structures
- alpha Helical Structures
- alpha-Helical Structure
|
Below are MeSH descriptors whose meaning is more general than "Protein Conformation, alpha-Helical".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation, alpha-Helical".
This graph shows the total number of publications written about "Protein Conformation, alpha-Helical" by people in this website by year, and whether "Protein Conformation, alpha-Helical" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2016 | 0 | 2 | 2 |
| 2017 | 2 | 22 | 24 |
| 2018 | 1 | 9 | 10 |
| 2019 | 0 | 10 | 10 |
| 2020 | 0 | 12 | 12 |
| 2021 | 0 | 7 | 7 |
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Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.
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In silico identification of novel SARS-COV-2 2'-O-methyltransferase (nsp16) inhibitors: structure-based virtual screening, molecular dynamics simulation and MM-PBSA approaches. J Enzyme Inhib Med Chem. 2021 Dec; 36(1):727-736.
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SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma. Proc Natl Acad Sci U S A. 2021 09 07; 118(36).
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Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles. J Am Chem Soc. 2021 08 25; 143(33):13205-13211.
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Broad betacoronavirus neutralization by a stem helix-specific human antibody. Science. 2021 09 03; 373(6559):1109-1116.
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V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity. J Virol. 2021 07 26; 95(16):e0061721.
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Membranotropic and biological activities of the membrane fusion peptides from SARS-CoV spike glycoprotein: The importance of the complete internal fusion peptide domain. Biochim Biophys Acta Biomembr. 2021 11 01; 1863(11):183697.
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Evolutionary insights into the furin cleavage sites of SARS-CoV-2 variants from humans and animals. Arch Virol. 2021 Sep; 166(9):2541-2549.
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Structural Analysis of the OC43 Coronavirus 2'-O-RNA Methyltransferase. J Virol. 2021 07 12; 95(15):e0046321.
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Can molecular mimicry explain the cytokine storm of SARS-CoV-2?: An in silico approach. J Med Virol. 2021 Sep; 93(9):5350-5357.
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Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies. Structure. 2021 07 01; 29(7):655-663.e4.