Stabilization of protein structure by solvents
1997; Oxford University Press; Linguagem: Inglês
10.1093/oso/9780199636198.003.0014
AutoresSerge N. Timasheff, Tsutomu Arakawa,
Tópico(s)Enzyme Structure and Function
ResumoAbstract It has been common practice for more than half a century for biochemists and biologists, when they have isolated an activity (e.g. an enzyme) or an organelle, to store the isolated material in concentrated (- 1 M) glycerol, sucrose, or a similar substance, in order to preserve this activity. Certain salts, such as ammonium sulfate, have also been known for a long time to stabilize biological activity, when added at high concentration (- J M). Yet the mechanism of such protein structure stabilization was totally unknown. At present, the manufacture of proteins, or modified proteins, by biosynthetic cloning technology has greatly revived interest in methods that are available for folding proteins into proper biologically active structures and for maintaining them in such a structure for prolonged periods. This chapter will be devoted to the question of the physical basis of the stabilization of native protein structures in aqueous solution by the addition of co-solvents at high (- 1 M) concentration. Such understanding should make it possible to use such co solvents rationally and effectively.
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