English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Single-molecule tracking of myosins with genetically engineered amplifier domains

Ruff, C., Furch, M., Brenner, B., Manstein, D. J., & Meyhöfer, E. (2001). Single-molecule tracking of myosins with genetically engineered amplifier domains. Nature Structural and Molecular Biology, 8(3), 226-229. doi:10.1038/84962.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Single-molecule tracking of myosins with genetically engineered amplifier domains

Files

show Files
hide Files
:
NatStructBiol_8_2001_226.pdf (Any fulltext), 574KB
 
File Permalink:
-
Name:
NatStructBiol_8_2001_226.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:
-

Locators

show
hide
Description:
-
OA-Status:
Locator:
http://dx.doi.org/10.1038/84962 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Ruff, Christine, Author
Furch, Marcus1, Author           
Brenner, Bernhard, Author
Manstein, Dietmar J.1, 2, Author           
Meyhöfer, Edgar, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              

Content

show
hide
Free keywords: -
 Abstract: We combined protein engineering and single molecule measurements to directly record the step size of a series of myosin constructs with shortened and elongated artificial neck domains. Our results show that the step size has a clear linear dependence on the length of the neck domain and we also established that mechanical amplification in the myosin motor is based on a rotation of the neck domain relative to the actin-bound head. For all our constructs, including those with artificial necks, the magnitude of the neck rotation concurrent with the displacement step was approximately 30 degrees. The engineered change in the step size of myosin marks a significant advance in our ability to selectively modify the functional properties of molecular motors.

Details

show
hide
Language(s): eng - English
 Dates: 2000-06-082000-12-012001-03-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 8 (3) Sequence Number: - Start / End Page: 226 - 229 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763