Pushing myocardial crossbridges to the limit: nonlinear kinetics of cardiac acto-myosin mechanics at large amplitudes of filament sliding

Author

Hunter, William C.

Author_Institution

Dept. of Biomed. Eng., Johns Hopkins Univ., Baltimore, MD, USA

Volume

1

fYear

1995

fDate

20-25 Sep 1995

Firstpage

85

Abstract

This study demonstrated that a crossbridge model incorporating multiple shortening steps per ATP hydrolysis cycle is consistent with experimental observations of myocardial dynamic stiffness for oscillation amplitudes that are large (i.e., up to 6%) relative to the molecular scale. Such a model also appears consistent with cardiac energetics, and may offer an improved representation of myocardial actomyosin kinetics

Keywords

biocontrol; biomechanics; cardiology; cellular transport; molecular biophysics; muscle; physiological models; proteins; ATP hydrolysis cycle; cardiac acto-myosin mechanics; cardiac energetics; filament sliding large amplitudes; molecular scale; multiple shortening steps; myocardial crossbridges; myocardial dynamic stiffness; nonlinear kinetics; oscillation amplitudes; Biomedical engineering; Biomedical measurements; Energy measurement; Kinetic theory; Mechanical variables measurement; Muscles; Myocardium; Performance analysis; Systems engineering and theory; Time measurement;

fLanguage

English

Publisher

ieee

Conference_Titel

Engineering in Medicine and Biology Society, 1995., IEEE 17th Annual Conference

Conference_Location

Montreal, Que.

Print_ISBN

0-7803-2475-7

Type

conf

DOI

10.1109/IEMBS.1995.575012

Filename

575012