Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase.

Abstract:

:The folding of the enzyme indole-3-glycerol-phosphate synthase (IGPS), a member of the (alpha/beta)8 fold family, has been studied. At least two folding intermediates have been detected using spectroscopic and activity measurements in combination with gel filtration chromatography. These two intermediates are produced by parallel pathways of a nonsequential unfolding mechanism rather than being consecutive steps in a sequential process. One intermediate can be detected in unfolding experiments because it is kinetically trapped in that conformation, but it is not observed in refolding experiments. It has spectroscopic and hydrodynamic properties very similar to those of the native protein, but it is inactive. The other intermediate could not be characterized because it either aggregates or unfolds under our experimental conditions and could not be isolated chromatographically.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Sánchez del Pino MM,Fersht AR

doi

10.1021/bi963133z

subject

Has Abstract

pub_date

1997-05-06 00:00:00

pages

5560-5

issue

18

eissn

0006-2960

issn

1520-4995

pii

bi963133z

journal_volume

36

pub_type

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