NDLI: Fluorescence Depolarization of Actin Filaments in Reconstructed Myofibers: The Effect of S1 or pPDM-S1 on Movements of Distinct Areas of Actin

Content Provider	PubMed Central
Author	Borovikov, Yu S. Dedova, I. V. Remedios, C. G. Dos Vikhoreva, N. N. Vikhorev, P. G. Avrova, S. V. Hazlett, T. L. Meer, B. W. Van Der
Copyright Year	2004
Abstract	Fluorescence polarization measurements were used to study changes in the orientation and order of different sites on actin monomers within muscle thin filaments during weak or strong binding states with myosin subfragment-1. Ghost muscle fibers were supplemented with actin monomers specifically labeled with different fluorescent probes at Cys-10, Gln-41, Lys-61, Lys-373, Cys-374, and the nucleotide binding site. We also used fluorescent phalloidin as a probe near the filament axis. Changes in the orientation of the fluorophores depend not only on the state of acto-myosin binding but also on the location of the fluorescent probes. We observed changes in polarization (i.e., orientation) for those fluorophores attached at the sites directly involved in myosin binding (and located at high radii from the filament axis) that were contrary to the fluorophores located at the sites close to the axis of thin filament. These altered probe orientations suggest that myosin binding alters the conformation of F-actin. Strong binding by myosin heads produces changes in probe orientation that are opposite to those observed during weak binding.
Starting Page	3020
File Format	PDF
ISSN	15420086
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	5
Volume Number	86
Language	English
Publisher	Biophysical Society
Publisher Date	2004-05-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Effect of Tropomyosin on Formin-Bound Actin Filaments

Fluorescence Depolarization Studies of Filamentous Actin Analyzed with a Genetic Algorithm

Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm–Tn chain

Assembly of Actin Filaments Studied by Laser Light Scattering and Fluorescence Photobleaching Recovery

Tropomyosin isoforms segregate into distinct clusters on single actin filaments

Mechanical Distortion of Single Actin Filaments Induced by External Force: Detection by Fluorescence Imaging

Velocity of movement of actin filaments in in vitro motility assay. Measured by fluorescence correlation spectroscopy.

On Phosphate Release in Actin Filaments

Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes.

Fluorescence Depolarization of Actin Filaments in Reconstructed Myofibers: The Effect of S1 or pPDM-S1 on Movements of Distinct Areas of Actin

Similar Documents

Effect of Tropomyosin on Formin-Bound Actin Filaments

Fluorescence Depolarization Studies of Filamentous Actin Analyzed with a Genetic Algorithm

Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm–Tn chain

Assembly of Actin Filaments Studied by Laser Light Scattering and Fluorescence Photobleaching Recovery

Tropomyosin isoforms segregate into distinct clusters on single actin filaments

Mechanical Distortion of Single Actin Filaments Induced by External Force: Detection by Fluorescence Imaging

Velocity of movement of actin filaments in in vitro motility assay. Measured by fluorescence correlation spectroscopy.

On Phosphate Release in Actin Filaments

Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes.

Fluorescence Depolarization of Actin Filaments in Reconstructed Myofibers: The Effect of S1 or pPDM-S1 on Movements of Distinct Areas of Actin