Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
International journal of food science & technology
30 (1995), S. 0
ISSN:
1365-2621
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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 thermostability. I also indicate the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulphide bridges make to thermostability.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1995.tb01364.x
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