Role of hydrophobic interactions in protein chain folding during biosynthesis

被引：0
|
作者：
Trikulenko, AV [1 ]
机构：
[1] Lviv Franko State Univ, UA-290005 Lviv, Ukraine
来源：
BIOCHEMISTRY-MOSCOW | 1998年 / 63卷 / 05期
关键词：
hydrophobic nuclei; hydrophobic potentials; hydrophobic interactions; protein chain folding;
D O I：
暂无
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：
It has been found that hydrophobic potentials of 30- to 40-amino acid fragments of amino acid sequences of myoglobin, cytochrome b(5), alpha-chymotrypsin, and seven other globular proteins analyzed are similar and correspond to free energies of formation of limited hydrophobic nuclei.
引用
收藏
页码：564 / 567
页数：4
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