Protein Structure, Tertiary
"Protein Structure, Tertiary" 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.
The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.
Descriptor ID |
D017434
|
MeSH Number(s) |
G02.111.570.820.709.610
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Concept/Terms |
Protein Structure, Tertiary- Protein Structure, Tertiary
- Tertiary Protein Structure
- Protein Structures, Tertiary
- Tertiary Protein Structures
|
Below are MeSH descriptors whose meaning is more general than "Protein Structure, Tertiary".
Below are MeSH descriptors whose meaning is more specific than "Protein Structure, Tertiary".
This graph shows the total number of publications written about "Protein Structure, Tertiary" by people in this website by year, and whether "Protein Structure, Tertiary" 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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1995 | 0 | 2 | 2 |
1996 | 0 | 1 | 1 |
1997 | 0 | 1 | 1 |
1999 | 0 | 1 | 1 |
2000 | 0 | 10 | 10 |
2001 | 0 | 15 | 15 |
2002 | 0 | 20 | 20 |
2003 | 0 | 19 | 19 |
2004 | 0 | 28 | 28 |
2005 | 2 | 32 | 34 |
2006 | 0 | 27 | 27 |
2007 | 0 | 22 | 22 |
2008 | 0 | 16 | 16 |
2009 | 1 | 26 | 27 |
2010 | 1 | 23 | 24 |
2011 | 1 | 28 | 29 |
2012 | 1 | 19 | 20 |
2013 | 0 | 22 | 22 |
2014 | 0 | 18 | 18 |
2015 | 0 | 17 | 17 |
2016 | 0 | 1 | 1 |
2017 | 0 | 5 | 5 |
2018 | 0 | 4 | 4 |
2019 | 0 | 1 | 1 |
2020 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein Structure, Tertiary" by people in Profiles.
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Li J, Davis I, Griffith WP, Liu A. Formation of Monofluorinated Radical Cofactor in Galactose Oxidase through Copper-Mediated C-F Bond Scission. J Am Chem Soc. 2020 11 04; 142(44):18753-18757.
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Stenzoski NE, Zou J, Piserchio A, Ghose R, Holehouse AS, Raleigh DP. The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models. Biochemistry. 2020 09 15; 59(36):3290-3299.
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Caldwell JT, Mermelstein DJ, Walker RC, Bernstein SI, Huxford T. X-ray Crystallographic and Molecular Dynamic Analyses of Drosophila melanogaster Embryonic Muscle Myosin Define Domains Responsible for Isoform-Specific Properties. J Mol Biol. 2020 01 17; 432(2):427-447.
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Chitrala KN, Yang X, Nagarkatti P, Nagarkatti M. Comparative analysis of interactions between aryl hydrocarbon receptor ligand binding domain with its ligands: a computational study. BMC Struct Biol. 2018 12 06; 18(1):15.
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Wang Y, Griffith WP, Li J, Koto T, Wherritt DJ, Fritz E, Liu A. Cofactor Biogenesis in Cysteamine Dioxygenase: C-F Bond Cleavage with Genetically Incorporated Unnatural Tyrosine. Angew Chem Int Ed Engl. 2018 07 02; 57(27):8149-8153.
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Alphonse S, Ghose R. Methyl NMR spectroscopy: Measurement of dynamics in viral RNA-directed RNA polymerases. Methods. 2018 09 15; 148:100-114.
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Vlaar CP, Castillo-Pichardo L, Medina JI, Marrero-Serra CM, V?lez E, Ramos Z, Hern?ndez E. Design, synthesis and biological evaluation of new carbazole derivatives as anti-cancer and anti-migratory agents. Bioorg Med Chem. 2018 02 15; 26(4):884-890.
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Serrano M, Gonzalez V, Ray S, Chavez MD, Narayan M. Identification of Structure-Stabilizing Interactions in Enzymes: A Novel Mechanism to Impact Enzyme Activity. Cell Biochem Biophys. 2018 Jun; 76(1-2):59-71.
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Ramos-Ben?tez MJ, Ruiz-Jim?nez C, Aguayo V, Espino AM. Recombinant Fasciola hepatica fatty acid binding protein suppresses toll-like receptor stimulation in response to multiple bacterial ligands. Sci Rep. 2017 07 14; 7(1):5455.
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Jennings S, Chenevert M, Liu L, Mottamal M, Wojcik EJ, Huckaba TM. Characterization of kinesin switch I mutations that cause hereditary spastic paraplegia. PLoS One. 2017; 12(7):e0180353.