Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.
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ABSTRACT:
SUBMITTER: Sugimoto H
PROVIDER: S-EPMC2776959 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Publications
Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.
Sugimoto Hayuki H Nakaura Miho M Nishimura Shigenori S Karita Shuichi S Miyake Hideo H Tanaka Akiyoshi A
Protein science : a publication of the Protein Society 20090801 8
Refolding of a thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase was investigated using differential scanning calorimetry, isothermal titration calorimetry, CD, and (1)H NMR. When the protein solution was rapidly cooled from a higher temperature, a kinetic intermediate was formed during refolding. The intermediate was unexpectedly stable compared with typical folding intermediates that have short half-lives. It was shown that this intermediate contained s ...[more]
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