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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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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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description	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.
doi_str_mv	10.1074/jbc.R111.275578
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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
title	Analysis and Functional Prediction of Reactive Cysteine Residues
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