蛋白质半胱氨酸残基各种修饰的鉴定分析  

Identification analysis of various modifications on cysteines

作　　者：邵囡 张锴[1] 何锡文[1] 张玉奎[2] 

机构地区：[1]南开大学化学学院,天津300071 [2]中国科学院大连化学物理研究所,辽宁大连116023

出　　处：《中国科技论文在线》2011年第12期916-920,共5页

基　　金：国家自然科学基金资助项目(20975053/U0932001)

摘　　要：通过采用蛋白质组学方法分析酵母家族蛋白激酶的研究中发现:半胱氨酸残基上存在多种蛋白修饰形式,其中3种可能为蛋白质翻译后修饰,9种可能来自于体外反应,主要由体外的化学衍生反应生成。通过二级质谱数据解析和生物信息学方法,研究了激酶家族蛋白质半胱氨酸残基上修饰的种类和化学结构,以及可能的反应过程,并对这些修饰出现的频率进行了归类分析。Cysteine has the reductive thiol functional group, The cysteine residues in protein are prone to oxidation and participate in some nuclephilic reactions. With the analytical methods ofproteomics, various modifications are discovered on cysteine, three of which might be the post-translational modifications and nine might be chemical reactions in vitro, especially some chemical derivations. Moreover, we investigated the types and the chemical structures of the modifications, possible reaction processes through MS/MS interpretations combined with bioinformatic analysis, and made statistical classifications on their frequencies.

关 键 词：分析化学 半胱氨酸 修饰 质谱 

分 类 号：O629.73[理学—有机化学]