DEHYDRATION-INDUCED CONFORMATIONAL TRANSITIONS IN PROTEINS AND THEIR INHIBITION BY STABILIZERS
DEHYDRATION-INDUCED CONFORMATIONAL TRANSITIONS IN PROTEINS AND THEIR INHIBITION BY STABILIZERS
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DOI：
10.1016/s0006-3495(93)81120-2
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发表时间：
1993-08-01
影响因子：
3.4
通讯作者：
CARPENTER, JF
中科院分区：
文献类型：
--
作者：
PRESTRELSKI, SJ;TEDESCHI, N;CARPENTER, JF
Dehydration of proteins results in significant, measurable conformational changes as observed using Fourier-transform infrared spectroscopy and resolution-enhancement techniques. For several proteins these conformational changes are at least partially irreversible, since, upon rehydration, denaturation and aggregation are observed. The presence of certain stabilizers inhibited these dehydration-induced transitions; the native structure was preserved in the dried state and upon reconstitution. Conformational transitions were also observed in a model polypeptide, poly-L-lysine, after lyophilization and were inhibited with the addition of stabilizing cosolutes. The ability of a particular additive to preserve the aqueous structure of dehydrated proteins and poly-L-lysine upon dehydration correlates directly with its ability to preserve the activity of lactate dehydrogenase, a labile enzyme, during drying.
