Journal ArticleDOI
Disulphide bridges in globular proteins
TLDR
There is a strong preference for shorter connections, with half-cystines separated by less than 24 residues in 49% of all disulphides.About:
This article is published in Journal of Molecular Biology.The article was published on 1981-09-15. It has received 747 citations till now. The article focuses on the topics: Globular protein.read more
Citations
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Stereochemical quality of protein structure coordinates.
TL;DR: The parameters used in this evaluation are not novel, and are easily calculated from structure coordinates, which provide a simple guide as to the reliability of a structure, in addition to the most important measures, resolution and R‐factor.
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Stability of Protein Pharmaceuticals
TL;DR: Current methodology to stabilize proteins is presented, including additives, excipients, chemical modification, and the use of site-directed mutagenesis to produce a more stable protein species.
Journal ArticleDOI
The changing faces of glutathione, a cellular protagonist
TL;DR: The significance of GSH as a major factor in regulation of cell life, proliferation, and death, should be regarded as the integrated result of all these roles it can play.
Journal ArticleDOI
Strategies for achieving high-level expression of genes in Escherichia coli.
TL;DR: Progress in the understanding of several biological processes promises to broaden the usefulness of Escherichia coli as a tool for gene expression and the remarkable increase in the availability of fusion partners offers a wide range of tools for improved protein folding, solubility, protection from proteases, yield, and secretion into the culture medium.
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Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
TL;DR: The redox potential of OxyR was determined to be -185 millivolts, ensuring that OxyR is reduced in the absence of stress as mentioned in this paper, which represents an example of redox signaling through disulfide bond formation and reduction.
References
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Journal ArticleDOI
The Protein Data Bank: a computer-based archival file for macromolecular structures.
Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
Journal ArticleDOI
Structural patterns in globular proteins
Michael Levitt,Cyrus Chothia +1 more
TL;DR: A simple diagrammatic representation has been used to show the arrangement of α helices and β sheets in 31 globular proteins, which are classified into four clearly separated classes.
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The nature of the accessible and buried surfaces in proteins
TL;DR: The accessible surface areas have been calculated for the individual residues in 12 proteins, and for the extended chains, the secondary structures and tertiary structure of six proteins and it is shown that the accessible surface area of folded proteins is simply proportional to the two-thirds power of their molecular weight.
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Structural invariants in protein folding.
Cyrus Chothia,Cyrus Chothia +1 more
TL;DR: An analysis of 15 protein structures indicates: first, the loss of accessible surface area by monomeric proteins on folding—proportional to hydrophobic energy—is a simple function of molecular weight.
Journal ArticleDOI
Conformation of amino acid side-chains in proteins.
Joël Janin,Shoshanna Wodak +1 more
TL;DR: Configurations that are rare for exposed residues are even rarer for buried residues, suggesting that, while the folded structure puts little strain on side-chain conformations, the side- chain positions with the lowest energy in the unfolded structure are chosen preferentially during folding.