A review of protein engineering for the food industry
1995
Goodenough, P.W.
In this review I briefly indicate how the present state of knowledge allows proteins to be mutated to increase or decrease stability. I discuss experiments on both model proteins and those of relevance to the food industry and show how hydrophobic forces are a major driving force for folding as well as having a major role in thermos/ability. I also indicate the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulphide bridges make to thermos/ability.
显示更多 [+] 显示较少 [-]AGROVOC关键词
书目信息
International journal of food science & technology
卷
30
期
2
页码
119
- 139
ISSN
0950-5423
其它主题
Molecular conformation; Sulfides (organic); Disulphide bridges; Electrostatic interactions; Hydrogen bonding
语言
英语
注释
2019-12-05
类型
Journal Article; Text
2024-02-28
MODS