Bacterial Proteins Fold Faster than Eukaryotic Proteins with Simple Folding Kinetics

被引：5
|
作者：
Galzitskaya, O. V. [1 ]
Bogatyreva, N. S. [1 ]
Glyakina, A. V. [2 ]
机构：
[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia
[2] Russian Acad Sci, Inst Math Problems Biol, Pushchino 142290, Moscow Region, Russia
来源：
BIOCHEMISTRY-MOSCOW | 2011年 / 76卷 / 02期
关键词：
all-or-none" transition; eukaryotic and bacterial proteins; folding intermediates; folding rate; protein folding; AMINO-ACID-SEQUENCE; SINGLE-DOMAIN PROTEINS; CONTACT ORDER; CHAIN-LENGTH; SECONDARY STRUCTURE; 2-STATE PROTEINS; RATE PREDICTION; RATES; TIME; MECHANISMS;
D O I：
10.1134/S000629791102009X
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Protein domain frequency and distribution among kingdoms was statistically analyzed using the SCOP structural database. It appeared that among chosen protein domains with the best resolution, eukaryotic proteins more often belong to alpha-helical and beta-structural proteins, while proteins of bacterial origin belong to alpha/beta structural class. Statistical analysis of folding rates of 73 proteins with known experimental data revealed that bacterial proteins with simple kinetics (23 proteins) exhibit a higher folding rate compared to eukaryotic proteins with simple folding kinetics (27 proteins). Analysis of protein domain amino acid composition showed that the frequency of amino acid residues in proteins of eukaryotic and bacterial origin is different for proteins with simple and complex folding kinetics.
引用
收藏
页码：225 / 235
页数：11
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