Intramolecular disulfide loop formation in a peptide containing two cysteines.

Abstract:

:The cyanogen bromide fragment comprising residues 115-181 of Kunitz soybean trypsin inhibitor is a soluble random-coil peptide at pH 7 containing two cysteines separated by eight other amino acids in the primary sequence. Four of the six rate constants have been determined for the three disulfide exchange reactions between this fragment and oxidized and reduced forms of N-acetylcysteine methyl ester. The rate constant for intramolecular loop formation in the fragment containing one thiolate anion and one sulfur connected by a disulfide bond to the small cysteine analogue is 0.36 +/- 0.15 s-1 at 23 degrees C in 3 M guanidine hydrochloride. This measurement provides a frame of reference corresponding to formation of a small but sterically unstrained loop, the fast limit for intramolecular disulfide exchange in a random-coil peptide.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Snyder GH

doi

10.1021/bi00377a005

subject

Has Abstract

pub_date

1987-02-10 00:00:00

pages

688-94

issue

3

eissn

0006-2960

issn

1520-4995

journal_volume

26

pub_type

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