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 |
|---|
| 2017 | 0 | 5 | 5 |
| 2018 | 0 | 1 | 1 |
| 2019 | 0 | 4 | 4 |
| 2020 | 0 | 3 | 3 |
| 2021 | 0 | 2 | 2 |
| 2024 | 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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Rational Design of TDP-43 Derived a-Helical Peptide Inhibitors: An In Silico Strategy to Prevent TDP-43 Aggregation in Neurodegenerative Disorders. ACS Chem Neurosci. 2024 03 20; 15(6):1096-1109.
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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.
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Discovery and characterization of bromodomain 2-specific inhibitors of BRDT. Proc Natl Acad Sci U S A. 2021 03 02; 118(9).
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Molecular dynamics, residue network analysis, and cross-correlation matrix to characterize the deleterious missense mutations in GALE causing galactosemia III. Cell Biochem Biophys. 2021 Jun; 79(2):201-219.
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HEPN RNases - an emerging class of functionally distinct RNA processing and degradation enzymes. Crit Rev Biochem Mol Biol. 2021 02; 56(1):88-108.
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KPC-2 ?-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate. J Biol Chem. 2021 Jan-Jun; 296:100155.
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Orsay Virus CP-d Adopts a Novel ?-Bracelet Structural Fold and Incorporates into Virions as a Head Fiber. J Virol. 2020 10 14; 94(21).
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Calmodulin-Calcineurin Interaction beyond the Calmodulin-Binding Region Contributes to Calcineurin Activation. Biochemistry. 2019 10 01; 58(39):4070-4085.
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Structural basis for preferential binding of human TCF4 to DNA containing 5-carboxylcytosine. Nucleic Acids Res. 2019 09 19; 47(16):8375-8387.
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Structural basis of specific DNA binding by the transcription factor ZBTB24. Nucleic Acids Res. 2019 09 19; 47(16):8388-8398.