Analysis and Functional Prediction of Reactive Cysteine Residues

Cys is much different from other common amino acids in proteins. Being one of the least abundant residues, Cys is often observed in functional sites in proteins. This residue is reactive, polarizable, and redox-active; has high affinity for metals; and is particularly responsive to the local environ...

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Bibliographic Details
Published in:The Journal of biological chemistry 2012-02, Vol.287 (7), p.4419-4425
Main Authors: Marino, Stefano M., Gladyshev, Vadim N.
Format: Article
Language:English
Subjects:
Algorithms
Animals
Computational Biology
Cysteine - chemistry
Cysteine - genetics
Cysteine-mediated Cross-linking
Disulfide
Humans
Minireviews
Oxidation-Reduction
Protein Structure
Proteins - chemistry
Proteins - genetics
Redox Regulation
Selenocysteine
Sequence Analysis, Protein - methods
Thioredoxin
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Summary:Cys is much different from other common amino acids in proteins. Being one of the least abundant residues, Cys is often observed in functional sites in proteins. This residue is reactive, polarizable, and redox-active; has high affinity for metals; and is particularly responsive to the local environment. A better understanding of the basic properties of Cys is essential for interpretation of high-throughput data sets and for prediction and classification of functional Cys residues. We provide an overview of approaches used to study Cys residues, from methods for investigation of their basic properties, such as exposure and pKa, to algorithms for functional prediction of different types of Cys in proteins.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.R111.275578