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.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
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2017 | 0 | 4 | 4 | 2018 | 0 | 1 | 1 | 2019 | 0 | 1 | 1 | 2020 | 0 | 2 | 2 | 2021 | 0 | 2 | 2 | 2023 | 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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Rosas R, Aguilar RR, Arslanovic N, Seck A, Smith DJ, Tyler JK, Churchill MEA. A novel single alpha-helix DNA-binding domain in CAF-1 promotes gene silencing and DNA damage survival through tetrasome-length DNA selectivity and spacer function. Elife. 2023 07 11; 12.
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Showers WM, Leach SM, Kechris K, Strong M. Longitudinal analysis of SARS-CoV-2 spike and RNA-dependent RNA polymerase protein sequences reveals the emergence and geographic distribution of diverse mutations. Infect Genet Evol. 2022 01; 97:105153.
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Cantrell MS, Wall JD, Pu X, Turner M, Woodbury L, Fujise K, McDougal OM, Warner LR. Expression and purification of a cleavable recombinant fortilin from Escherichia coli for structure activity studies. Protein Expr Purif. 2022 01; 189:105989.
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Sarkar A, Kim EY, Jang T, Hongdusit A, Kim H, Choi JM, Fox JM. Microbially Guided Discovery and Biosynthesis of Biologically Active Natural Products. ACS Synth Biol. 2021 06 18; 10(6):1505-1519.
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Laursen SP, Bowerman S, Luger K. Archaea: The Final Frontier of Chromatin. J Mol Biol. 2021 03 19; 433(6):166791.
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Zatopek KM, Alpaslan E, Evans TC, Sauguet L, Gardner AF. Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases. Nucleic Acids Res. 2020 12 02; 48(21):12204-12218.
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Liu J, Xue Z, Zhang Y, Vann KR, Shi X, Kutateladze TG. Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1. Structure. 2020 11 03; 28(11):1225-1230.e3.
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Panda AK, Chakraborty A, Nandi SK, Biswas A. The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3. Proteins. 2020 06; 88(6):759-774.
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Song K, Li Q, Gao W, Lu S, Shen Q, Liu X, Wu Y, Wang B, Lin H, Chen G, Zhang J. AlloDriver: a method for the identification and analysis of cancer driver targets. Nucleic Acids Res. 2019 07 02; 47(W1):W315-W321.
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Mant CT, Jiang Z, Gera L, Davis T, Nelson KL, Bevers S, Hodges RS. De Novo Designed Amphipathic a-Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii. J Med Chem. 2019 04 11; 62(7):3354-3366.
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