Document Detail


Effect of nucleotides and their analogues on essential light chains in myosin head.
MedLine Citation:
PMID:  12406588     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The domain movement in myosin head plays a decisive role in the energy transduction process of the muscle contraction. During hydrolysis of ATP, the specific formation of strong binding of myosin head for actin causes conformational changes. As a consequence, the light chain-binding motif generates the powerstroke. In our work maleimide spin labels were covalently attached to Cys-177 residue of ELC in subfragment-1 (S1). Our goal was to study the orientation dependence and the motion of S1, which were incorporated into glycerinated skeletal muscle fibres. The electron paramagnetic resonance spectroscopy (EPR) spectra of the probes depended strongly on the orientation of the fibre axis relative to the magnetic field, indicating that the essential light chain (ELC) and the neck were ordered. The probes were undergoing rapid motion within a cone. The half-width of the cone was estimated to be 65+/-5 degrees (SD, n=8). Addition of ADP affected little the hyperfine splitting and the angular spread of the probe distribution. In the presence of ADP and orthovanadate the intensity of the spectra decreased, which showed the dissociation of S1 and this was accompanied with the disappearance of the orientation dependence.
Authors:
Nóra Hartvig; Balázs Gaszner; Márta Kiss; Dénes Lorinczy; Joseph Belágyi
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Publication Detail:
Type:  Comparative Study; Evaluation Studies; In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Validation Studies    
Journal Detail:
Title:  Journal of biochemical and biophysical methods     Volume:  53     ISSN:  0165-022X     ISO Abbreviation:  J. Biochem. Biophys. Methods     Publication Date:    2002 Oct-Nov
Date Detail:
Created Date:  2002-10-30     Completed Date:  2003-09-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7907378     Medline TA:  J Biochem Biophys Methods     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  67-74     Citation Subset:  IM    
Affiliation:
Central Research Laboratory, Faculty of Medicine, University of Pécs, 12 Szigeti Str., H-7643 Pécs, Hungary.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Diphosphate / chemistry*,  metabolism
Animals
Computer Simulation
Electron Spin Resonance Spectroscopy / methods*
Maleimides
Models, Molecular
Molecular Motor Proteins / chemistry*,  metabolism
Molecular Probe Techniques
Motion
Muscle Fibers, Skeletal / chemistry*,  metabolism
Muscle, Skeletal
Myosin Light Chains / chemistry,  metabolism
Myosin Subfragments / chemistry,  metabolism
Myosins / chemistry*,  metabolism
Nucleotides / chemistry,  metabolism
Protein Structure, Tertiary
Psoas Muscles
Rabbits
Spin Labels
Chemical
Reg. No./Substance:
0/Maleimides; 0/Molecular Motor Proteins; 0/Myosin Light Chains; 0/Myosin Subfragments; 0/Nucleotides; 0/Spin Labels; 541-59-3/maleimide; 58-64-0/Adenosine Diphosphate; EC 3.6.4.1/Myosins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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