Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths

Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths

At a resting sarcomere length of approximately 2.2 µm bony fish muscles put into rigor in the presence of BDM (2,3-butanedione monoxime) to reduce rigor tension generation show the normal arrangement of myosin head interactions with actin filaments as monitored by low-angle X-ray diffracti...

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Bibliographic Details
Main Authors: Felicity Eakins, Jeffrey J. Harford, Carlo Knupp, Manfred Roessle, John M. Squire
Format: Article
Language:English
Published: MDPI AG 2018-07-01
Series:International Journal of Molecular Sciences
Subjects:
rigor muscle
myosin cross-bridge cycle
steric blocking mechanism
roll and lock mechanism
low-angle X-ray diffraction
synchrotron radiation
bony fish muscle
Online Access:http://www.mdpi.com/1422-0067/19/7/2091

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http://www.mdpi.com/1422-0067/19/7/2091

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