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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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
MeSH Number(s)	G02.111.570.820.709.600.020
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".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Molecular Structure [G02.111.570]
Molecular Conformation [G02.111.570.820]
Protein Conformation [G02.111.570.820.709]
Protein Structure, Secondary [G02.111.570.820.709.600]
Protein Conformation, alpha-Helical [G02.111.570.820.709.600.020]

Below are MeSH descriptors whose meaning is related to "Protein Conformation, alpha-Helical".

Below are MeSH descriptors whose meaning is more specific than "Protein Conformation, alpha-Helical".

publications

Timeline | Most Recent

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.

Bar chart showing 17 publications over 8 distinct years, with a maximum of 4 publications in 2020

To see the data from this visualization as text, click here.

Year	Minor Topic	Total
2016	1	1
2017	3	3
2018	3	3
2019	2	2
2020	4	4
2021	2	2
2022	1	1
2024	1	1

Below are the most recent publications written about "Protein Conformation, alpha-Helical" by people in Profiles.

Ye W, Krishna Behra PR, Dyrhage K, Seeger C, Joiner JD, Karlsson E, Andersson E, Chi CN, Andersson SGE, Jemth P. Folded Alpha Helical Putative New Proteins from Apilactobacillus kunkeei. J Mol Biol. 2024 03 15; 436(6):168490.

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Zhang J, Walker ME, Sanidad KZ, Zhang H, Liang Y, Zhao E, Chacon-Vargas K, Yeliseyev V, Parsonnet J, Haggerty TD, Wang G, Simpson JB, Jariwala PB, Beaty VV, Yang J, Yang H, Panigrahy A, Minter LM, Kim D, Gibbons JG, Liu L, Li Z, Xiao H, Borlandelli V, Overkleeft HS, Cloer EW, Major MB, Goldfarb D, Cai Z, Redinbo MR, Zhang G. Microbial enzymes induce colitis by reactivating triclosan in the mouse gastrointestinal tract. Nat Commun. 2022 01 10; 13(1):136.

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Maben Z, Arya R, Georgiadis D, Stratikos E, Stern LJ. Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism. Nat Commun. 2021 09 06; 12(1):5302.

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Schmidt EJ, Funes S, McKeon JE, Morgan BR, Boopathy S, O'Connor LC, Bilsel O, Massi F, J?gou A, Bosco DA. ALS-linked PFN1 variants exhibit loss and gain of functions in the context of formin-induced actin polymerization. Proc Natl Acad Sci U S A. 2021 06 08; 118(23).

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Karlsson E, Paissoni C, Erkelens AM, Tehranizadeh ZA, Sorgenfrei FA, Andersson E, Ye W, Camilloni C, Jemth P. Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins. J Biol Chem. 2020 12 18; 295(51):17698-17712.

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Chan YH, Zeldovich KB, Matthews CR. An allosteric pathway explains beneficial fitness in yeast for long-range mutations in an essential TIM barrel enzyme. Protein Sci. 2020 09; 29(9):1911-1923.

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Vreven T, Vangaveti S, Borrman TM, Gaines JC, Weng Z. Performance of ZDOCK and IRAD in CAPRI rounds 39-45. Proteins. 2020 08; 88(8):1050-1054.

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Hayes JA, Hilbert BJ, Gaubitz C, Stone NP, Kelch BA. A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry. J Biol Chem. 2020 03 20; 295(12):3783-3793.

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Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG. Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure. 2019 12 03; 27(12):1782-1797.e7.

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Karlsson E, Andersson E, Jones NC, Hoffmann SV, Jemth P, Kjaergaard M. Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism. Biophys J. 2019 08 20; 117(4):729-742.

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