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 | 0 | 1 | 1 |
| 2018 | 0 | 5 | 5 |
| 2019 | 0 | 2 | 2 |
| 2020 | 0 | 1 | 1 |
| 2021 | 0 | 2 | 2 |
| 2022 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.
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Inhibition of FOXP3 by stapled alpha-helical peptides dampens regulatory T cell function. Proc Natl Acad Sci U S A. 2022 10 18; 119(42):e2209044119.
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Serine 408 phosphorylation is a molecular switch that regulates structure and function of the occludin a-helical bundle. Proc Natl Acad Sci U S A. 2022 08 23; 119(34):e2204618119.
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Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin. J Am Chem Soc. 2021 11 03; 143(43):18073-18090.
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Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB. Protein Sci. 2021 09; 30(9):1904-1918.
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Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. Protein Sci. 2020 07; 29(7):1596-1605.
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Identification of Antibodies Targeting the H3N2 Hemagglutinin Receptor Binding Site following Vaccination of Humans. Cell Rep. 2019 12 24; 29(13):4460-4470.e8.
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Development of "Plug and Play" Fiducial Marks for Structural Studies of GPCR Signaling Complexes by Single-Particle Cryo-EM. Structure. 2019 12 03; 27(12):1862-1874.e7.
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Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering. J Phys Chem B. 2019 03 07; 123(9):2016-2021.
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Structure of Calcarisporiella thermophila Hsp104 Disaggregase that Antagonizes Diverse Proteotoxic Misfolding Events. Structure. 2019 03 05; 27(3):449-463.e7.
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A Membrane Burial Potential with H-Bonds and Applications to Curved Membranes and Fast Simulations. Biophys J. 2018 11 20; 115(10):1872-1884.