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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

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.

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Abstract

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 ...

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Item Type:Article
Date:1991
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
1868084PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
AnimalsMESH
Escherichia coli/geneticsMESH
HydrogenMESH
Hydrogen-Ion ConcentrationMESH
Magnetic Resonance Spectroscopy/methodsMESH
Molecular Sequence DataMESH
Myosin Subfragments/geneticsMESH
Myosins/chemistryMESH
Peptide Fragments/chemistryMESH
Protein ConformationMESH
RabbitsMESH
Recombinant Proteins/chemistryMESH
X-Ray Diffraction/methodsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:07 Sep 2010 06:18
Last Modified:07 Sep 2010 06:18
Item ID:16460
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