Lysine reactivities of tropomyosin complexed with troponin

Sarah E. Hitchcock-DeGregori, Stephen F. Lewis, Mark Mistrik

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The relative reactivities of lysine residues of tropomyosin complexed with troponin have been measured in order to locate the binding site of troponin on tropomyosin in a complex between the two native proteins. The lysines were labeled with acetic anhydride using a competitive labeling procedure and the relative reactivities of tropomyosin lysine containing peptides were compared to those from tropomyosin labeled in the absence of troponin (S. E. Hitchcock-DeGregori, S. F. Lewis, and T. M.-T. Chou, (1985) Biochemistry 24, 3305-3314). Analysis of about two-thirds of the lysines indicates that troponin affects the reactivities of lysines along the length of the tropomyosin, indicating long-range effects. The inferred binding site is more extensive than previously reported, about 25 nm, extending from res. 136 to the carboxy-terminus and to res. 30 beyond the end-to-end overlap in the amino-terminal region of the next tropomyosin molecule.

Original languageEnglish (US)
Pages (from-to)410-416
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Aug 1988

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology


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