Analysis of cooperativity observed in pH titrations of proton nuclear magnetic resonances of histidine residues of rabbit cardiac tropomyosin.

Abstract:

:We have investigated in detail the cooperativity which we had previously observed in the pH titration profiles of the histidine residues of rabbit tropomyosin [Edwards, B. F. P., & Sykes, B. D. (1978) Biochemistry 17, 684]. Nonpolymerizing tropomyosin was prepared by carboxypeptidase digestion, and the titration profiles of its histidine residues were compared with those of undigested tropomyosin which was fully polymerized (in 0.1 M KCl) throughout the titration. We have concluded that both histidine-153 and histidine-273 have significant cooperativity in their pH titrations only in polymerized tropomyosin, that the cooperativity arises from an intrinsic pH-dependent conformational transition which links the two residues together and not from the known pH dependence of the polymerization, and that the best model for the cooperativity is a biallosteric adaption of the Monod--Wyman--Changeux formalism involving two classes of binding sites for the same ligand (protons). Three other models which postulated either a Hill transition, an interaction with a neighboring residue that also titrates, or a pH-dependent polymerization were also considered.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Edwards BF,Sykes BD

doi

10.1021/bi00517a037

subject

Has Abstract

pub_date

1981-07-07 00:00:00

pages

4193-8

issue

14

eissn

0006-2960

issn

1520-4995

journal_volume

20

pub_type

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