Open AccessAmino acid sequence of a myosin fragment that contains SH-1, SH-2, and Ntau-methylhistidine.
Author(s) -
Marshall Elzinga,
John H. Collins
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.10.4281
Subject(s) - cyanogen bromide , myosin , peptide , peptide sequence , biochemistry , amino acid , myosin head , chemistry , actin , stereochemistry , protein primary structure , biology , myosin light chain kinase , gene
A peptide having 92 amino acid residues and a calculated molecular weight of 10,478 was isolated from a cyanogen bromide digest of rabbit skeletal muscle myosin. It contained both proline and Ntau-methylhistidine, indicating that it arose from the portion of the heavy chain that folds to form most of the globular head of the myosin molecule. The amino acid sequence of the peptide included the two sulfhydryl groups whose alkylation modifies myosin's catalytic properties: SH-2 at position 11 in the peptide, and SH-1 at position 21. This proximity in the sequence means that SH-1 and SH-2 must be relatively close together in myosin, and several lines of evidence suggest that this region is near the catalytic or actin binding site(s) of myosin.