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.
|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-Stranded Structures
- beta Stranded Structures
- beta-Stranded Structure
- beta Strand
- beta Sheet
- beta-Pleated Sheet
- Sheet, beta-Pleated
- Sheets, beta-Pleated
- beta Pleated Sheet
- beta-Pleated 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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Below are the most recent publications written about "Protein Conformation, beta-Strand" by people in Profiles.
Engineering ?-Sheet Peptide Coassemblies for Biomaterial Applications. J Phys Chem B. 2021 12 23; 125(50):13599-13609.
Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB. Protein Sci. 2021 09; 30(9):1904-1918.
Glycosylation of a Nonfibrillizing Appendage Alters the Self-Assembly Pathway of a Synthetic ?-Sheet Fibrillizing Peptide. J Phys Chem B. 2021 06 24; 125(24):6559-6571.
CATCH Peptides Coassemble into Structurally Heterogeneous ?-Sheet Nanofibers with Little Preference to ?-Strand Alignment. J Phys Chem B. 2021 04 29; 125(16):4004-4015.
Atomic-level differences between brain parenchymal- and cerebrovascular-seeded A? fibrils. Sci Rep. 2021 01 08; 11(1):247.
Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. Protein Sci. 2020 07; 29(7):1596-1605.
Anatomy of a selectively coassembled ?-sheet peptide nanofiber. Proc Natl Acad Sci U S A. 2020 03 03; 117(9):4710-4717.
Molecular complementarity and structural heterogeneity within co-assembled peptide ?-sheet nanofibers. Nanoscale. 2020 Feb 21; 12(7):4506-4518.
Identification of Antibodies Targeting the H3N2 Hemagglutinin Receptor Binding Site following Vaccination of Humans. Cell Rep. 2019 12 24; 29(13):4460-4470.e8.
Development of "Plug and Play" Fiducial Marks for Structural Studies of GPCR Signaling Complexes by Single-Particle Cryo-EM. Structure. 2019 12 03; 27(12):1862-1874.e7.