Kalbitzer, Hans Robert and Maeda, K. and Rösch, A. and Maéda, Y. and Geyer, M. and Beneicke, W. and Neidig, K. P. and Wittinghofer, A. (1991) C-terminal structure and mobility of rabbit skeletal muscle light meromyosin as studied by one- and two-dimensional ¹H NMR spectroscopy and X-ray small-angle scattering. Biochemistry 30 (32), pp. 8083-8091.
Full text not available from this repository.
Intact rabbit myosin and two different C-terminal fragments of rabbit muscle light meromyosin (LMM) expressed in Escherichia coli, LMM-30, and LMM-30C', were studied by 1H NMR spectroscopy. X-ray small-angle scattering shows that at high ionic strength two polypeptide chains of LMM-30 (which consists of the C-terminal 262 amino acids of myosin heavy chain) or LMM-30C' (which corresponds to LMM-30 ...
Export bibliographical data
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Dewey Decimal Classification:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||07 Sep 2010 06:18|
|Last Modified:||07 Sep 2010 06:18|