Ca2+-induced conformational changes in the troponin complex detected by crosslinking

Nikolay B. Gusev, P. Friedrich

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In an attempt to detect Ca2+-induced conformational changes by crosslinking, rabbit muscle troponin complex was reacted with the bifunctional reagents 1,3-difluoro-4,6-dinitrobenzene, 4,4′-difluoro-3,3′-dinitrodiphenylsulfone and dimethyl suberimidate under various conditions and the products were analyzed by dodecyl sulfate gel electrophoresis. In the absence of divalent cations, with the two aromatic reagents at a low reagent/protein ratio, the main crosslink products were troponin T-I and I-C. With dimethyl suberimidate the only major crosslink product was conjugate T-I. Ca2+, alone as well as in the presence of Mg2+, prevented the formation of I-C crosslinks with both aromatic reagents, but it did not affect crosslinking with dimethyl suberimidate. Ca2+ also decreased the number of NH2 groups of troponin that are highly reactive towards 2,4,6-trinitrobenzene sulfonate. Both effects of Ca2+ can be interpreted in terms of a conformational change in the troponin complex elicited by the binding of the specific divalent cation.

Original languageEnglish
Pages (from-to)106-116
Number of pages11
JournalBBA - Protein Structure
Volume626
Issue number1
DOIs
Publication statusPublished - Nov 20 1980

Fingerprint

Dimethyl Suberimidate
Troponin
Crosslinking
Divalent Cations
Trinitrobenzenesulfonic Acid
Cross-Linking Reagents
Troponin T
Troponin I
Electrophoresis
Muscle
Gels
Rabbits
Muscles
Proteins

Keywords

  • Amino group reactivity
  • Ca binding
  • Conformational change
  • Crosslinking
  • Troponin complex

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Ca2+-induced conformational changes in the troponin complex detected by crosslinking. / Gusev, Nikolay B.; Friedrich, P.

In: BBA - Protein Structure, Vol. 626, No. 1, 20.11.1980, p. 106-116.

Research output: Contribution to journalArticle

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