English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by (1)H NMR spectroscopy

MPS-Authors
/persons/resource/persons93660

Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1016/S0014-5793%2802%2902855-7
(Any fulltext)

https://doi.org/10.1016/S0014-5793(02)02855-7
(Any fulltext)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Kany, H., Wolf, J., & Kalbitzer, H. R. (2002). Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by (1)H NMR spectroscopy. FEBS Letters, 521(1), 121-126. doi:10.1016/S0014-5793(02)02855-7.


Cite as: https://hdl.handle.net/21.11116/0000-0001-EF78-C
Abstract
Mg-F-actin occurs in two conformational states, I and M, where the N-terminal amino acids are either immobile or highly mobile. In the rigor or ADP complex of rabbit myosin S1 with Mg-F-actin the N-terminal acetyl group of actin stays in its highly mobile state. The same is true for the complexes with the myosin motor domain from Dictyostelium discoideum. This excludes a direct strong interaction of the N-terminal amino acids with myosin in the rigor state as suggested. An interaction of the N-terminus of F-actin with myosin is also not promoted by occupying its low-affinity binding site(s) with divalent ions. The N-terminal high-mobility region may be part of a structural system which has evolved for releasing inadequate stress applied to the actin filaments.