Studies on actomyosin crossbridge flexibility using a new single molecule assay.

Several key flexure sites exist in the muscle crossbridge including the actomyosin binding site which play important roles in the actomyosin crossbridge cycle. To distinguish between these sources of flexibility, a new single molecule assay was developed to observe the swiveling of rod about a single myosin. Myosins attached through a single crossbridge displayed mostly similar torsional characteristics compared to myosins attached through two crossbridges, which indicates that most of the torsional flexibility resides in the myosin subfragment-2, and thus the hinge between subfragment-2 and light meromyosin should contribute the most to this flexibility. The comparison of torsional characteristics in the absence and presence of ADP demonstrated a small but significant increase in twist rates for the double-headed myosins but no increase for single-headed myosins, which indicates that the ADP-induced increase in flexibility arises due to changes in the myosin head and verifies that most flexibility resides in myosin subfragment-2.

Grantor dc:publisher

University of North Texas

Year dc:date

2004

Author dc:creator

• Gundapaneni, Deepika

Contributors dc:contributor

• Root, Douglas D.
• Chapman, Kent D.
• Padilla, Pamela

• Actomyosin.
• torsional flexibility
• actomyosin
• crossbridge
• single molecule assay
• ADP

Statement dc:rights

• Public
• Copyright
• Gundapaneni, Deepika
• Copyright is held by the author, unless otherwise noted. All rights reserved.

Language dc:language

English

Identifier

oclc: 55665751
https://digital.library.unt.edu/ark:/67531/metadc4514/
ark: ark:/67531/metadc4514

OAI identifier oai:identifier

info:ark/67531/metadc4514