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.
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
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| MeSH Number(s) |
G02.111.570.820.709.600.750
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| 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".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation, beta-Strand".
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.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2017 | 0 | 1 | 1 |
| 2018 | 0 | 1 | 1 |
| 2019 | 1 | 1 | 2 |
| 2020 | 0 | 2 | 2 |
| 2021 | 0 | 4 | 4 |
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Below are the most recent publications written about "Protein Conformation, beta-Strand" by people in Profiles.
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Structural and phylogenetic analyses of resistance to next-generation aminoglycosides conferred by AAC(2') enzymes. Sci Rep. 2021 06 02; 11(1):11614.
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Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation. Nat Chem Biol. 2021 05; 17(5):615-623.
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Direct Observation of ?-Barrel Intermediates in the Self-Assembly of Toxic SOD128-38 and Absence in Nontoxic Glycine Mutants. J Chem Inf Model. 2021 02 22; 61(2):966-975.
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Probing Interdomain Linkers and Protein Supertertiary Structure In Vitro and in Live Cells with Fluorescent Protein Resonance Energy Transfer. J Mol Biol. 2021 03 05; 433(5):166793.
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aB-Crystallin Chaperone Inhibits A? Aggregation by Capping the ?-Sheet-Rich Oligomers and Fibrils. J Phys Chem B. 2020 11 12; 124(45):10138-10146.
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Thermo- and pH-responsive fibrillization of squid suckerin A1H1 peptide. Nanoscale. 2020 Mar 21; 12(11):6307-6317.
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Dynamic allostery-based molecular workings of kinase:peptide complexes. Proc Natl Acad Sci U S A. 2019 07 23; 116(30):15052-15061.
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Amyloid Self-Assembly of hIAPP8-20 via the Accumulation of Helical Oligomers, a-Helix to ?-Sheet Transition, and Formation of ?-Barrel Intermediates. Small. 2019 05; 15(18):e1805166.
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?-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-? Aggregates. Sci Rep. 2018 07 09; 8(1):10353.
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Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA-recognition motif. Acta Crystallogr F Struct Biol Commun. 2017 04 01; 73(Pt 4):209-214.