The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein.

Abstract:

:Domains are in general less stable than the corresponding full-length proteins. Human utrophin tandem calponin-homology (CH) domain seems to be an exception. Reversible, equilibrium denaturant melts indicate that the isolated C-terminal domain (CH2) is thermodynamically more stable than the tandem CH domain. Thermal melts show that CH2 unfolds at a temperature higher than that at which the full-length protein unfolds. Stopped-flow kinetics indicates that CH2 unfolds slower than the full-length protein, indicating its higher kinetic stability. Thus, the utrophin tandem CH domain may be one of the few proteins in which an isolated domain is more stable than the corresponding full-length protein.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bandi S,Singh SM,Mallela KM

doi

10.1021/bi500120e

subject

Has Abstract

pub_date

2014-04-15 00:00:00

pages

2209-11

issue

14

eissn

0006-2960

issn

1520-4995

journal_volume

53

pub_type

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