THE STABILIZATION OF PROTEINS BY OSMOLYTES
THE STABILIZATION OF PROTEINS BY OSMOLYTES
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DOI:
10.1016/s0006-3495(85)83932-1
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发表时间:
1985-01-01
影响因子:
3.4
通讯作者:
TIMASHEFF, SN
中科院分区:
文献类型:
--
作者:
ARAKAWA, T;TIMASHEFF, SN
The preferential interactions of lysozyme with solvent components, and the effects of solvent additives on its stability were examined for several neutral osmolytes: L-proline, L-serine, GABA acid, sarcosine, taurine, .alpha.-alanine, .beta.-alanine, glycine, betaine, and trimethylamine N-oxide. All these substances stabilize protein structure against thermal denaturation, and (except for trimethylamine N-oxide, for which interaction measurements could not be made) they are strongly excluded from the protein domain, rendering unlikely their direct binding to proteins. Valine, not known as an osmolyte, had no stabilizing effect, although it induced a large protein-preferential hydration. A possible explanation is given for the use of these substances as osmotic-pressure-regulating agents in organisms living under high osmotic pressure.