English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides

Menetret, J. F., Hofmann, W. F., Schröder, R. R., Rapp, G., & Goody, R. S. (1991). Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides. Journal of Biological Chemistry, 219(2), 139-144. doi:10.1016/0022-2836(91)90554-J.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-ACCD-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-730E-0
Genre: Journal Article

Files

show Files
hide Files
:
JMolBiol_219_1991_139.pdf (Any fulltext), 9MB
 
File Permalink:
-
Name:
JMolBiol_219_1991_139.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Menetret, J. F., Author
Hofmann, W. F., Author
Schröder, Rasmus R.1, 2, Author           
Rapp, Gert, Author
Goody, Roger S.2, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: time-resolved cryo-electron microscopy; caged nucleotides; actomyosin; actin
 Abstract: The rapid release of a substrate or other ligand from photolabile precursors in a thin layer suspension of biological specimens followed by rapid freezing provides a method of trapping and visualizing short-lived states in a dynamic system. We demonstrate here the first successful application of this method to study the interaction of actin filaments with myosin subfragment 1 (S1) after release of nucleotides. The results obtained suggest that structural changes in actin filaments occur as a result of interaction with S1.

Details

show
hide
Language(s): eng - English
 Dates: 1990-04-201991-02-032005-03-091991-05-20
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0022-2836(91)90554-J
URI: https://www.ncbi.nlm.nih.gov/pubmed/2038049
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 219 (2) Sequence Number: - Start / End Page: 139 - 144 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826