Protein Conformation, beta-Strand

"Protein Conformation, beta-Strand" 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 where the amino (N-H) groups of a polypeptide backbone, three to ten amino acids in length, establish hydrogen bonds with the carbonyl (C=O) groups in the backbone of adjacent strands. These may form a beta-sheet, where the side chains of the adjacent strands point in the same direction.

Descriptor ID	D000072757
MeSH Number(s)	G02.111.570.820.709.600.750
Concept/Terms	Protein Conformation, beta-Strand Protein Conformation, beta-Strand Conformation, beta-Strand Protein Conformations, beta-Strand Protein Protein Conformation, beta Strand Protein Conformations, beta-Strand beta-Strand Protein Conformation beta-Strand Protein Conformations beta-Strands beta Strands beta-Stranded Structures beta Stranded Structures beta-Stranded Structure beta-Strand beta Strand beta-Sheet beta-Sheet beta Sheet beta-Pleated Sheet Sheet, beta-Pleated Sheets, beta-Pleated beta Pleated Sheet beta-Pleated Sheets beta-Sheets beta Sheets Protein Conformation, beta-Sheet Conformation, beta-Sheet Protein Conformations, beta-Sheet Protein Protein Conformation, beta Sheet Protein Conformations, beta-Sheet beta-Sheet Protein Conformation beta-Sheet Protein Conformations

Below are MeSH descriptors whose meaning is more general than "Protein Conformation, beta-Strand".

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, beta-Strand [G02.111.570.820.709.600.750]

Below are MeSH descriptors whose meaning is related to "Protein Conformation, beta-Strand".

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

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Protein Conformation, beta-Strand" by people in this website by year, and whether "Protein Conformation, beta-Strand" was a major or minor topic of these publications.

Bar chart showing 9 publications over 6 distinct years, with a maximum of 2 publications in 2017 and 2019 and 2020

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

Year	Major Topic	Minor Topic	Total
2017	0	2	2
2018	1	0	1
2019	0	2	2
2020	0	2	2
2021	0	1	1
2022	0	1	1

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

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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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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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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Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, F?ndrich M, Schmidt M. Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. Nat Commun. 2019 03 07; 10(1):1104.

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Close W, Neumann M, Schmidt A, Hora M, Annamalai K, Schmidt M, Reif B, Schmidt V, Grigorieff N, F?ndrich M. Physical basis of amyloid fibril polymorphism. Nat Commun. 2018 02 16; 9(1):699.

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Malaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG. Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors. Structure. 2018 01 02; 26(1):106-117.e6.

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Shrimal S, Cherepanova NA, Gilmore R. One flexible loop in OST lassos both substrates. Nat Struct Mol Biol. 2017 12 07; 24(12):1009-1010.

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Shi J, Nobrega RP, Schwantes C, Kathuria SV, Bilsel O, Matthews CR, Lane TJ, Pande VS. Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY. Sci Rep. 2017 03 08; 7:44116.

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