The study of 3-D structure and dynamic property of G-actin by molecular mechanics simulation

Author

Nakamachi, Eiji

Author_Institution

Dept. of Mech. Eng. for Comput.-Controlled Machinery, Osaka Univ., Japan

fYear

1994

fDate

1994

Firstpage

738

Abstract

To understand the micro-mechanism of muscle contraction, the structure and dynamic property of G-actin is studied by introducing the molecular mechanics simulation code AMBER. The minimum energy conformation and compressibility are investigated under four conditions, the combination of G-actin or proK-actin and with or without ATP. These studies show G-actin under the similar condition to in vivo has least energy and largest compressibility. It might mean better functional ability to generate the muscle contractile motion

Keywords

molecular biophysics; molecular configurations; muscle; proteins; ATP; G-actin 3D structure; G-actin dynamic property; molecular mechanics simulation; molecular mechanics simulation code AMBER; muscle contractile motion generation; muscle contraction micromechanism; proK-actin; protein dynamics; protein structure; Atomic measurements; Bonding; Computational modeling; Computer simulation; Fluctuations; Gradient methods; Mechanical factors; Muscles; Potential energy; Vibrations;

fLanguage

English

Publisher

ieee

Conference_Titel

Engineering in Medicine and Biology Society, 1994. Engineering Advances: New Opportunities for Biomedical Engineers. Proceedings of the 16th Annual International Conference of the IEEE

Conference_Location

Baltimore, MD

Print_ISBN

0-7803-2050-6

Type

conf

DOI

10.1109/IEMBS.1994.415268

Filename

415268