Bending of smooth muscle myosin rod.

Abstract:

:Electron microscopy of mammalian smooth muscle myosin rods showed them to be 153 +/- 7 nm (SD) long, and to bend sharply (greater than 90 degrees) but infrequently, and pH independently (range 6.5-9.5), at a single site 45 +/- 4 nm from one end of the molecule. Light meromyosin (LMM) preparations were 99 +/- 10 nm long, and showed no bends. Intrinsic viscosity vs temperature plots for rods and LMM indicated that neither fragment changed in flexibility in the range 4-40 degrees C. Peptide mapping in the presence and absence of SDS established that the proteolytic susceptibility of the hinge at the N terminus of LMM reflects the presence of locally different structure, and not simply a clustering of susceptible residues. The isolated smooth muscle myosin rod thus contains only a single hinge, having significant stiffness, and lacks the second bend seen under certain conditions in the intact molecule.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Cross RA

doi

10.1016/0014-5793(84)80940-0

subject

Has Abstract

pub_date

1984-10-15 00:00:00

pages

197-201

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)80940-0

journal_volume

176

pub_type

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