Loop fold structure of proteins: Resolution of Levinthal's paradox

被引：41
作者：
Berezovsky, IN
Trifonov, EN
机构：
[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel
[2] Univ Haifa, Genome Divers Ctr, Inst Evolut, IL-31905 Haifa, Israel
来源：
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2002年 / 20卷 / 01期
关键词：
Levinthal's paradox; protein folding; chain conformation; closed loops; loop fold structure;
D O I：
10.1080/07391102.2002.10506817
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：
According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins - 25-30 residues.
引用
收藏
页码：5 / 6
页数：2
相关论文
共 9 条
1