Harvard Catalyst Profiles

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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 motifs) pack together to form folded shapes called domains. 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. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.


This graph shows the total number of publications written about "Protein Structure, Tertiary" by people in Harvard Catalyst Profiles by year, and whether "Protein Structure, Tertiary" was a major or minor topic of these publication.
Bar chart showing 3353 publications over 28 distinct years, with a maximum of 256 publications in 2004
To see the data from this visualization as text, click here.
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Funded by the NIH/NCATS Clinical and Translational Science Award (CTSA) program, grant number UL1TR001102, and through institutional support from Harvard University, Harvard Medical School, Harvard T.H. Chan School of Public Health, Beth Israel Deaconess Medical Center, Boston Children's Hospital, Brigham and Women's Hospital, Massachusetts General Hospital and the Dana Farber Cancer Institute.