Electronic Resource
Springer
Journal of inclusion phenomena and macrocyclic chemistry
25 (1996), S. 85-88
ISSN:
1573-1111
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The energetics of interaction of a range of cyclodextrins with folded and unfolded proteins has been examined by sensitive microcalorimetry techniques. Weak interaction with exposed amino acid residues promotes unfolding and dissociation of proteins. The possibility that such interactions may facilitate the use of cyclodextrins as “chaperone-mimics” in the refolding of denatured protein has been explored with the enzyme phosphoglycerate kinase. Up to 40% regain of activity can be achieved in some cases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01041542
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