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A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism.

Abstract：

:Above pH 6, swine pepsin undergoes a conformational change to a neutral form which has 80% of the secondary structure of the native protein. In contrast to native pepsin, this form of the enzyme can be reversibly unfolded by urea in a rapid, cooperative reaction. Since all of pepsin's sequence is present in its precursor pepsinogen, it is likely that this neutral structure is present in one or more of the transient intermediates previously detected in the reversible unfolding reaction of the zymogen. The mechanism of this rapid reaction may resemble early steps in protein folding.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

McPhie P

doi

10.1016/s0006-291x(89)80185-8

subject

Has Abstract

pub_date

1989-01-16 00:00:00

pages

115-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(89)80185-8

journal_volume

158

pub_type

杂志文章

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