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Activity and conformational changes of α‐chymotrypsin in reverse micelles studied by spin labeling
Author(s) -
Marzola P.,
Forte C.,
Pinzino C.,
Veracini C.A.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80901-e
Subject(s) - micelle , chemistry , chymotrypsin , aqueous solution , site directed spin labeling , spin probe , substrate (aquarium) , spin label , dynamics (music) , crystallography , photochemistry , enzyme , trypsin , organic chemistry , biochemistry , biology , physics , membrane , acoustics , ecology
α‐Chymotrypsin (CT), spin‐labeled at the active site by using an acylating label which constitutes a substrate for this protein, has been investigated in reverse micelles formed by AOT in isooctane. The electron spin resonance spectra provided information on conformation, dynamics and deacylation activity. The dynamics of the label bound to CT appears to be more hindered in reverse micelles than in aqueous solution, probably owing to the effect of the micellar environment on protein conformation. The deacylation rate in reverse micelles does not show the characteristic bell‐shaped dependence on water content which is generally found for CT enzymatic activity.