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PMID: 1489906 Published · ppublish English Journal Article

Structure of the myosin head in solution and the effect of light chain 2 removal.

Biophysical journal ·Vol. 63 ·No. 6 ·1992-12-00 ·Pages 1462-70

Garrigos M, Mallam S, Vachette P, Bordas J

Abstract

Structural properties of rabbit skeletal myosin head (S1) and the influence of the DTNB light chain (LC2) on the size and shape of myosin heads in solution were investigated by small angle x-ray scattering. The LC2 deficient myosin head, S1 (-LC2), and the S1 containing LC2 light chain, S1 (+LC2) were studied in parallel. The respective values of the radius of gyration were found to be (40.2 +/- 0.5) A and (46.7 +/- 1) A, while the maximum dimension was (190 +/- 15) A for both species. The large difference between the two Rg values suggest that LC2 is located close to one extremity of the myosin head, in agreement with most electron microscopy observations. All models derived from the x-ray scattering pattern of the native myosin head share a common overall morphology, showing two main regions, an asymmetric globular portion which tapers smoothly into a thinner domain of roughly equivalent length making an angle of approximately 60 degrees, with a contour length of approximately 210 A.

MeSH Terms
Animals Biophysical Phenomena Biophysics In Vitro Techniques Models, Molecular Molecular Structure Myosin Subfragments/chemistry,ultrastructure Myosins/chemistry,ultrastructure Protein Conformation Rabbits Scattering, Radiation Solutions X-Rays
Chemicals
Myosin Subfragments Solutions Myosins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Garrigos M
Département de Biologie, CEN-Saclay, Gif-sur-Yvette, France.
Mallam S
Vachette P
Bordas J
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1992-12-00
Pages
1462-70
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1262260
Subset
IM
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