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
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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.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
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2017 | 0 | 2 | 2 | 2019 | 0 | 1 | 1 | 2020 | 0 | 5 | 5 | 2021 | 0 | 1 | 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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Showers WM, Leach SM, Kechris K, Strong M. Longitudinal analysis of SARS-CoV-2 spike and RNA-dependent RNA polymerase protein sequences reveals the emergence and geographic distribution of diverse mutations. Infect Genet Evol. 2022 01; 97:105153.
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Cantrell MS, Wall JD, Pu X, Turner M, Woodbury L, Fujise K, McDougal OM, Warner LR. Expression and purification of a cleavable recombinant fortilin from Escherichia coli for structure activity studies. Protein Expr Purif. 2022 01; 189:105989.
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Laursen SP, Bowerman S, Luger K. Archaea: The Final Frontier of Chromatin. J Mol Biol. 2021 03 19; 433(6):166791.
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Alnaas AA, Watson-Siriboe A, Tran S, Negussie M, Henderson JA, Osterberg JR, Chon NL, Harrott BM, Oviedo J, Lyakhova T, Michel C, Reisdorph N, Reisdorph R, Shearn CT, Lin H, Knight JD. Multivalent lipid targeting by the calcium-independent C2A domain of synaptotagmin-like protein 4/granuphilin. J Biol Chem. 2021 Jan-Jun; 296:100159.
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Zatopek KM, Alpaslan E, Evans TC, Sauguet L, Gardner AF. Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases. Nucleic Acids Res. 2020 12 02; 48(21):12204-12218.
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Chaparro Sosa AF, de Oliveira da Silva SM, Morgan GP, Schwartz DK, Kaar JL. Mixed Phospholipid Vesicles Catalytically Inhibit and Reverse Amyloid Fibril Formation. J Phys Chem Lett. 2020 Sep 03; 11(17):7417-7422.
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Majewski J, Jones EM, Vander Zanden CM, Biernat J, Mandelkow E, Chi EY. Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein. Sci Rep. 2020 08 07; 10(1):13324.
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Liu J, Xue Z, Zhang Y, Vann KR, Shi X, Kutateladze TG. Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1. Structure. 2020 11 03; 28(11):1225-1230.e3.
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Panda AK, Chakraborty A, Nandi SK, Biswas A. The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3. Proteins. 2020 06; 88(6):759-774.
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Clayton GM, White J, Lee S, Kappler JW, Chan SK. Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6. PLoS One. 2019; 14(9):e0213052.
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