Intermediate states of myosin head during atp hydrolysis cycle in psoas muscle fibres by EPR and DSC: A review

Research output: Article

17 Citations (Scopus)

Abstract

Force generation in muscle during contraction arises from direct interaction of the two main protein components of the muscle, myosin and actin. The process is driven by the energy liberated from the hydrolysis of ATP. In the presence of CaATP the energy released from hydrolysis produces conformational changes in myosin and actin, which can be manifested as an internal motion of myosin head while bound to actin. It is suggested that myosin heads attached to actin produce conformational changes during the hydrolysis process of ATP, which results in a strain in the head portion of myosin in an ATP-dependent manner. These structural changes lead to a large rotation of myosin neck region relieving the strain. Paramagnetic probes and EPR spectroscopy provide direct method in which the rotation and orientation of specifically labelled proteins can be followed during muscle activity. In order to find correlation between local and global structural changes in the intermediate states of the ATPase cycle, the spectroscopic measurements were combined with DSC measurements that report domain stability and interactions. In the review a detailed description of the application of EPR and DSC techniques in muscle protein research will be given. The measurements show that the small local structural changes detected by EPR after nucleotide binding influence the global structure of protein system responsible for muscle contraction.

Original languageEnglish
Pages (from-to)611-621
Number of pages11
JournalJournal of Thermal Analysis and Calorimetry
Volume90
Issue number2
DOIs
Publication statusPublished - nov. 2007

Fingerprint

muscle fibers
myosins
Myosins
Paramagnetic resonance
Muscle
hydrolysis
Hydrolysis
Adenosinetriphosphate
cycles
Fibers
adenosine triphosphate
Actins
Proteins
Adenosine Triphosphate
muscles
muscular function
proteins
relieving
Nucleotides
Muscle Proteins

ASJC Scopus subject areas

  • Chemical Engineering(all)

Cite this

@article{cdccb6932a3e4245a6c4dc3f490a6ef8,
title = "Intermediate states of myosin head during atp hydrolysis cycle in psoas muscle fibres by EPR and DSC: A review",
abstract = "Force generation in muscle during contraction arises from direct interaction of the two main protein components of the muscle, myosin and actin. The process is driven by the energy liberated from the hydrolysis of ATP. In the presence of CaATP the energy released from hydrolysis produces conformational changes in myosin and actin, which can be manifested as an internal motion of myosin head while bound to actin. It is suggested that myosin heads attached to actin produce conformational changes during the hydrolysis process of ATP, which results in a strain in the head portion of myosin in an ATP-dependent manner. These structural changes lead to a large rotation of myosin neck region relieving the strain. Paramagnetic probes and EPR spectroscopy provide direct method in which the rotation and orientation of specifically labelled proteins can be followed during muscle activity. In order to find correlation between local and global structural changes in the intermediate states of the ATPase cycle, the spectroscopic measurements were combined with DSC measurements that report domain stability and interactions. In the review a detailed description of the application of EPR and DSC techniques in muscle protein research will be given. The measurements show that the small local structural changes detected by EPR after nucleotide binding influence the global structure of protein system responsible for muscle contraction.",
keywords = "DSC, EPR, Intermediate states of ATP hydrolysis, Muscle fibre",
author = "D. Lőrinczy and J. Bel{\'a}gyi",
year = "2007",
month = "11",
doi = "10.1007/s10973-006-7728-6",
language = "English",
volume = "90",
pages = "611--621",
journal = "Journal of Thermal Analysis and Calorimetry",
issn = "1388-6150",
publisher = "Springer Netherlands",
number = "2",

}

TY - JOUR

T1 - Intermediate states of myosin head during atp hydrolysis cycle in psoas muscle fibres by EPR and DSC

T2 - A review

AU - Lőrinczy, D.

AU - Belágyi, J.

PY - 2007/11

Y1 - 2007/11

N2 - Force generation in muscle during contraction arises from direct interaction of the two main protein components of the muscle, myosin and actin. The process is driven by the energy liberated from the hydrolysis of ATP. In the presence of CaATP the energy released from hydrolysis produces conformational changes in myosin and actin, which can be manifested as an internal motion of myosin head while bound to actin. It is suggested that myosin heads attached to actin produce conformational changes during the hydrolysis process of ATP, which results in a strain in the head portion of myosin in an ATP-dependent manner. These structural changes lead to a large rotation of myosin neck region relieving the strain. Paramagnetic probes and EPR spectroscopy provide direct method in which the rotation and orientation of specifically labelled proteins can be followed during muscle activity. In order to find correlation between local and global structural changes in the intermediate states of the ATPase cycle, the spectroscopic measurements were combined with DSC measurements that report domain stability and interactions. In the review a detailed description of the application of EPR and DSC techniques in muscle protein research will be given. The measurements show that the small local structural changes detected by EPR after nucleotide binding influence the global structure of protein system responsible for muscle contraction.

AB - Force generation in muscle during contraction arises from direct interaction of the two main protein components of the muscle, myosin and actin. The process is driven by the energy liberated from the hydrolysis of ATP. In the presence of CaATP the energy released from hydrolysis produces conformational changes in myosin and actin, which can be manifested as an internal motion of myosin head while bound to actin. It is suggested that myosin heads attached to actin produce conformational changes during the hydrolysis process of ATP, which results in a strain in the head portion of myosin in an ATP-dependent manner. These structural changes lead to a large rotation of myosin neck region relieving the strain. Paramagnetic probes and EPR spectroscopy provide direct method in which the rotation and orientation of specifically labelled proteins can be followed during muscle activity. In order to find correlation between local and global structural changes in the intermediate states of the ATPase cycle, the spectroscopic measurements were combined with DSC measurements that report domain stability and interactions. In the review a detailed description of the application of EPR and DSC techniques in muscle protein research will be given. The measurements show that the small local structural changes detected by EPR after nucleotide binding influence the global structure of protein system responsible for muscle contraction.

KW - DSC

KW - EPR

KW - Intermediate states of ATP hydrolysis

KW - Muscle fibre

UR - http://www.scopus.com/inward/record.url?scp=36849008065&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36849008065&partnerID=8YFLogxK

U2 - 10.1007/s10973-006-7728-6

DO - 10.1007/s10973-006-7728-6

M3 - Article

AN - SCOPUS:36849008065

VL - 90

SP - 611

EP - 621

JO - Journal of Thermal Analysis and Calorimetry

JF - Journal of Thermal Analysis and Calorimetry

SN - 1388-6150

IS - 2

ER -