PMID:9008296
| Citation |
Kim, JS and Kim, H (1996) Stability and folding of a mutant ribose-binding protein of Escherichia coli. J. Protein Chem. 15:731-6 |
|---|---|
| Abstract |
A mature mutant ribose-binding protein (RBP) of Escherichia coli was obtained by site-directed mutagenesis, replacing Thr-3 in the N-domain of wild-type mature RBP (WT-mRBP) with a Trp residue (N-Trp-mRBP). The equilibrium unfolding properties and the refolding kinetics of this protein were monitored by fluorescence and circular dichroism (CD). The stability of N-Trp-mRBP appears to be the same as that of C-Trp-mRBP, another mutant obtained by replacing Phe-187 with a Trp, and lower than that of WT-mRBP. The overall refolding rate of N-Trp-mRBP is much smaller than that of C-Trp-mRBP, which, in turn, is similar to that of WT-mRBP. For the case of WT-mRBP, the rate constant obtained by Tyr fluorescence is identical to the value obtained by CD. But with C-Trp-mRBP, the rate constant from CD is smaller than the value from the Trp fluorescence and this difference in the rate constants is much greater with the N-Trp-mRBP. |
| Links | |
| Keywords |
Carrier Proteins/chemistry; Circular Dichroism; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins; Guanidine; Guanidines/pharmacology; Kinetics; Models, Molecular; Mutagenesis, Site-Directed/genetics; Mutation/genetics; Periplasmic Binding Proteins; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan/metabolism |
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