Strong hydrophobic nature of cysteine residues in proteins
Strong hydrophobic nature of cysteine residues in proteins
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DOI：
10.1016/s0014-5793(99)01122-9
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发表时间：
1999-09-10
期刊：
影响因子：
3.5
通讯作者：
Nishikawa, K
中科院分区：
文献类型：
--
作者：
Nagano, N;Ota, M;Nishikawa, K
通过分析已知结构蛋白质中二硫键结合半胱氨酸(Cys_SS)和游离半胱氨酸(Cys_SH)残基的统计分布，比较了这两种残基的差异。令人惊讶的是，Cys_SH残基表现出比Cys_SS残基更强的疏水性，这是对与之接触的原子的详细调查。Cys_SH的巯基(硫原子)表明，这些原子与异亮氨酸的甲基在数量和种类上基本相同，但与丝氨酸的羟基有很大的不同，此外，还利用已知蛋白质结构的3D-Profile表确定了氨基酸之间的关系。Cys_SH与Met、Trp、Tyr等残基一起位于疏水基团中，在极性基团中与Ser、Thr明显分离，这些结果表明游离半胱氨酸在蛋白质中表现为强烈的疏水残基，而不是亲水残基，(C)1999欧洲生化学会联合会。
The differences between disulfide-bonding cystine (Cys_SS) and free cysteine (Cys_SH) residues were examined by analyzing the statistical distribution of both types of residue in proteins of known structure. Surprisingly, Cys_SH residues display stronger hydrophobicity than Cys_SS residues, A detailed survey of atoms which come into contact with. the sulfhydryl group (sulfur atom) of Cys_SH revealed those atoms are essentially the same in number and variety as those of the methyl group of isoleucine, but are quite different to those of the hydroxyl group of serine, Moreover, the relationships among amino acids were also determined using the 3D-profile table of known protein structures. Cys_SH was located in the hydrophobic cluster, along with residues such as Met, Trp and Tyr, and was clearly separated from Ser and Thr in the polar cluster, These results imply that free cysteines behave as strongly hydrophobic, and not hydrophilic, residues in proteins, (C) 1999 Federation of European Biochemical Societies.