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
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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 |
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2017 | 0 | 1 | 1 |
2019 | 0 | 1 | 1 |
2021 | 0 | 4 | 4 |
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Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.
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Structure-Function Analysis of Two Interacting Vaccinia Proteins That Are Critical for Viral Morphogenesis: L2 and A30.5. J Virol. 2022 01 26; 96(2):e0157721.
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Structural and phylogenetic analyses of resistance to next-generation aminoglycosides conferred by AAC(2') enzymes. Sci Rep. 2021 06 02; 11(1):11614.
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Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation. Nat Chem Biol. 2021 05; 17(5):615-623.
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Probing Interdomain Linkers and Protein Supertertiary Structure In Vitro and in Live Cells with Fluorescent Protein Resonance Energy Transfer. J Mol Biol. 2021 03 05; 433(5):166793.
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Dynamic allostery-based molecular workings of kinase:peptide complexes. Proc Natl Acad Sci U S A. 2019 07 23; 116(30):15052-15061.
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Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA-recognition motif. Acta Crystallogr F Struct Biol Commun. 2017 04 01; 73(Pt 4):209-214.