Deamidation of human proteins

被引：230

作者：

Robinson, NE ^{[1
]}

Robinson, AB

机构：

[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

[2] Oregon Inst Sci & Med, Cave Junction, OR 97523 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 22期

关键词：

in vivo deamidation; asparaginyl residues;

D O I：

10.1073/pnas.221463198

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Deamidation of asparaginyl and glutaminyl residues causes time-dependent changes in charge and conformation of peptides and proteins. Quantitative and experimentally verified predictive calculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 126 human proteins have been performed. These rates suggest that deamidation is a biologically relevant phenomenon in a remarkably large percentage of human proteins.

引用

页码：12409 / 12413

页数：5

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