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 |
|---|
| 2018 | 0 | 2 | 2 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.
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N-glycosylation and homodimeric folding significantly enhance the immunoreactivity of Mycobacterium tuberculosis virulence factor CFP32 when produced in the yeast Pichia pastoris. Biochem Biophys Res Commun. 2019 08 27; 516(3):845-850.
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An update on the biophysical character of the human eukaryotic elongation factor 1 beta: Perspectives from interaction with elongation factor 1 gamma. J Mol Recognit. 2018 07; 31(7):e2708.
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Hypothesis: apo-lactoferrin-Galantamine Proteo-alkaloid Conjugate for Alzheimer's disease Intervention. J Cell Mol Med. 2018 03; 22(3):1957-1963.