PROTEIN STABILITY - EXPERIMENTAL-DATA FROM PROTEIN ENGINEERING

被引：15

作者：

FERSHT, AR ^{[1
]}

JACKSON, SE ^{[1
]}

SERRANO, L ^{[1
]}

机构：

[1] DEPT CHEM, CAMBRIDGE, DORSET, ENGLAND

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES | 1993年 / 345卷 / 1674期

关键词：

D O I：

10.1098/rsta.1993.0125

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：

All of molecular recognition, from the binding of substrates by enzymes, information transfer in replicating and processing the genetic information to the folding of proteins, is dominated by non-covalent interactions. Perhaps the most difficult challenge is understanding protein folding because each group in the molecule has to recognize with which ones it has to pair. Protein engineering is providing and experimental entry to determine the magnitude, nature and importance of the various levels of recognition in protein folding. In addition to providing the energetics of specific interactions, fundamental information has been given on the energetics of burial of hydrophobic and hydrophilic solvent-accessible surface areas and their specific roles in stabilizing protein cores and helices.

引用

页码：141 / 151

页数：11

共 59 条

[31] ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING [J].