Document Detail


Analysis of nucleotide myosin complexes in skeletal muscle fibres by DSC and EPR.
MedLine Citation:
PMID:  12406589     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The internal dynamics and thermal unfolding of fibre bundles prepared from rabbit psoas muscle has been studied in the presence of nucleotides by differential scanning calorimetry (DSC) and electron paramagnetic resonance (EPR) spectroscopy. Using ADP, adenosine 5'-triphosphate (ATP), AMP.PNP and inorganic phosphate analogue orthovanadate (V(i)), AlF(4)(-) and BeF(3)(-), three intermediate states of the ATP hydrolysis cycle were simulated in glycerinated muscle fibres. In the main transition of the DSC pattern, three overlapping endotherms were detected in rigor, four in strongly as well as weakly binding state of myosin to actin. Deconvolution procedure showed that the transition temperature of 67.5 degrees C was the same for rigor and strong binding state of myosin. In contrast, nucleotide binding induced shift of the melting temperatures of 52 degrees C and 67.5 degrees C, appeared a new fourth peak at 74 and 77 degrees C and produced changes in the calorimetric enthalpies. The changes of the parameters of the peak functions suggest global rearrangements of the internal structure in myosin heads in the intermediate states. In the presence of ADP or ATP plus phosphate analogue orthovanadate or beryllium fluoride, aluminium fluoride, the conventional EPR spectra of spin-labeled muscle fibres showed large changes in the ordering of the probe molecules, and a new distribution of spin labels appeared. ATP plus orthovanadate induced the orientation disorder of myosin heads; the random population of spin labels gave evidence of large local conformational and motional changes in the internal structure of myosin heads. Saturation transfer EPR measurements reported increased rotational mobility of spin labels in the presence of ATP plus phosphate analogues corresponding to weakly binding state of myosin to actin.
Authors:
D Lorinczy; N Hartvig; J Belagyi
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Publication Detail:
Type:  Comparative Study; In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
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:  75-87     Citation Subset:  IM    
Affiliation:
Biophysical Department, Faculty of Medicine, University of Pécs, H-7624, Pécs, 12 Szigeti Str, Hungary. denes.lorinczy@aok.pte.edu
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MeSH Terms
Descriptor/Qualifier:
Actins / chemistry,  metabolism
Aluminum Compounds
Animals
Calorimetry, Differential Scanning / methods*
Electron Spin Resonance Spectroscopy / methods*
Fluorides
Hot Temperature
Kinetics
Macromolecular Substances
Molecular Motor Proteins / chemistry,  metabolism
Molecular Probe Techniques
Muscle Fibers, Skeletal / chemistry*,  metabolism
Myosins / chemistry*,  metabolism
Nucleotides / chemistry*,  metabolism
Phosphorus / chemistry,  metabolism
Protein Conformation
Protein Denaturation
Protein Folding
Psoas Muscles
Rats
Temperature
Vanadates
Chemical
Reg. No./Substance:
0/Actins; 0/Aluminum Compounds; 0/Fluorides; 0/Macromolecular Substances; 0/Molecular Motor Proteins; 0/Nucleotides; 0/Vanadates; 7723-14-0/Phosphorus; 7784-18-1/aluminum fluoride; EC 3.6.4.1/Myosins

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


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