Kany, Harry and Wolf, Jones and Kalbitzer, Hans Robert (2002) Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by ¹H NMR spectroscopy. FEBS letters 521 (1-3), pp. 121-126.
Full text not available from this repository.
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 ...
Export bibliographical data
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Subjects:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||15 Sep 2010 09:14|
|Last Modified:||15 Sep 2010 09:14|