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 |
|---|
| 2016 | 0 | 1 | 1 |
| 2018 | 0 | 2 | 2 |
| 2019 | 0 | 1 | 1 |
| 2020 | 0 | 3 | 3 |
| 2021 | 0 | 5 | 5 |
| 2023 | 0 | 1 | 1 |
| 2024 | 1 | 0 | 1 |
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Below are the most recent publications written about "Protein Conformation, beta-Strand" by people in Profiles.
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Parallel ß-Sheet Structure and Structural Heterogeneity Detected within Q11 Self-Assembling Peptide Nanofibers. J Phys Chem B. 2024 Jun 06; 128(22):5387-5396.
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Side-Chain Chemistry Governs Hierarchical Order of Charge-Complementary ß-sheet Peptide Coassemblies. Angew Chem Int Ed Engl. 2023 12 18; 62(51):e202314531.
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Engineering ß-Sheet Peptide Coassemblies for Biomaterial Applications. J Phys Chem B. 2021 12 23; 125(50):13599-13609.
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Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB. Protein Sci. 2021 09; 30(9):1904-1918.
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Glycosylation of a Nonfibrillizing Appendage Alters the Self-Assembly Pathway of a Synthetic ß-Sheet Fibrillizing Peptide. J Phys Chem B. 2021 06 24; 125(24):6559-6571.
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CATCH Peptides Coassemble into Structurally Heterogeneous ß-Sheet Nanofibers with Little Preference to ß-Strand Alignment. J Phys Chem B. 2021 04 29; 125(16):4004-4015.
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Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aß fibrils. Sci Rep. 2021 01 08; 11(1):247.
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Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. Protein Sci. 2020 07; 29(7):1596-1605.
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Anatomy of a selectively coassembled ß-sheet peptide nanofiber. Proc Natl Acad Sci U S A. 2020 03 03; 117(9):4710-4717.
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Molecular complementarity and structural heterogeneity within co-assembled peptide ß-sheet nanofibers. Nanoscale. 2020 Feb 21; 12(7):4506-4518.