Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
J Biol Chem. 2012 Feb 10;287(7):4419-25. doi: 10.1074/jbc.R111.275578. Epub 2011 Dec 6.
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 pK(a), to algorithms for functional prediction of different types of Cys in proteins.
半胱氨酸在蛋白质中与其他常见氨基酸有很大的不同。作为最不丰富的残基之一，半胱氨酸经常出现在蛋白质的功能位点中。这种残基具有反应性、极化性和氧化还原活性；对金属具有高亲和力；并且对局部环境特别敏感。对半胱氨酸基本性质的更好理解对于解释高通量数据集以及预测和分类蛋白质中的功能半胱氨酸残基是必要的。我们提供了一种研究半胱氨酸残基的方法概述，从研究其基本性质（如暴露度和 pK(a)）的方法到用于预测蛋白质中不同类型半胱氨酸功能的算法。
