Abstract
At the present time it is generally assumed that most, if not all, proteins possess well-defined structures. This assumption is based on several kinds of evidence: (1) the finding that many proteins have unique amino acid sequences, with specific intrachain disulfide bonds; (2) the ability to determine the three-dimensional configuration (tertiary structure) and, in some instances, even portions of the amino acid sequence of proteins such as myoglobin and hemoglobin by X-ray crystallographic methods; (3) the highly reproducible physical-chemical properties of a large number of proteins; and (4) the great degree of configurational specificity which appears necessary for enzymic activity. When one considers the complexity of the tertiary structure of a “native” protein, it seems reasonable to inquire into how a newly-made protein arrives at its three-dimensional configuration.
Keywords
Protein tertiary structureMyoglobinAmino acid residueChemistryProtein structureDisulfide bondAmino acidSequence (biology)Computational biologyPeptide sequenceProtein structure predictionHemoglobinCrystallographyBiochemistryBiologyGene
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Publication Info
- Year
- 1963
- Type
- article
- Volume
- 28
- Issue
- 0
- Pages
- 439-449
- Citations
- 304
- Access
- Closed
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Cite This
Charles J. Epstein,
Robert F. Goldberger,
Christian B. Anfinsen
(1963).
The Genetic Control of Tertiary Protein Structure: Studies With Model Systems.
Cold Spring Harbor Symposia on Quantitative Biology
, 28
(0)
, 439-449.
https://doi.org/10.1101/sqb.1963.028.01.060
Identifiers
- DOI
- 10.1101/sqb.1963.028.01.060