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Rabbit skeletal muscle myosin. Unfolded carboxyl-terminus and its role in molecular assembly

Maeda, K. and Rösch, A. and Maéda, Y. and Kalbitzer, Hans Robert and Wittinghofer, A. (1991) Rabbit skeletal muscle myosin. Unfolded carboxyl-terminus and its role in molecular assembly. FEBS letters 281 (1-2), pp. 23-26.

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Abstract

We have expressed in E. coli segments of the rod portion of rabbit skeletal fast muscle myosin and compared physical properties of two different species, LMM-30 and LMM-30C'. LMM-30 consists of 263 amino acids including the original C-terminus of myosin heavy chain. LMM-30C' is colinear with LMM-30, but is devoid of 17 residues at the C-terminus. 1H NMR spectroscopy indicates that the C-terminus ...

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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
2015900PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
AnimalsMESH
Base SequenceMESH
Genetic VectorsMESH
Magnetic Resonance Spectroscopy/methodsMESH
Molecular Sequence DataMESH
Muscles/metabolismMESH
Myosins/geneticsMESH
Oligonucleotide ProbesMESH
Protein ConformationMESH
RabbitsMESH
SolubilityMESH
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 06:22
Last Modified:07 Sep 2010 06:22
Item ID:16458
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