Amino acid sequence of a myosin fragment that contains SH-1, SH-2, and N/sup tau/-methylhistidine

Journal Article · Sat Oct 01 04:00:00 EDT 1977 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.74.10.4281· OSTI ID:6328383

Elzinga, M ^[1]; Collins, J H

---

1. Brookhaven National Lab., Upton, NY

A peptid 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 N/sup tau/-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.

• OSTI ID: 6328383
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 74:10; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALKYLATION
AMINO ACIDS
AZOLES
BIOCHEMICAL REACTION KINETICS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
GLOBULINS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
IMIDAZOLES
KINETICS
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
MYOSIN
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDES
PROTEINS
RADICALS
REACTION KINETICS
SULFHYDRYL RADICALS