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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 of LMM-30, but not of LMM-30C' is unfolded and freely mobile. Furthermore, the present results show that the unfolded C-terminus is essential for molecular assembly of LMM-30; at pH 8.0 LMM-30, but not LMM-30C', formed aggregates upon decreasing the ionic strength.

Item Type:

Article

Institutions:

Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer

Identification Number:

Value	Type
2015900	PubMed ID

Classification:

Notation	Type
Amino Acid Sequence	MESH
Animals	MESH
Base Sequence	MESH
Genetic Vectors	MESH
Magnetic Resonance Spectroscopy/methods	MESH
Molecular Sequence Data	MESH
Muscles/metabolism	MESH
Myosins/genetics	MESH
Oligonucleotide Probes	MESH
Protein Conformation	MESH
Rabbits	MESH
Solubility	MESH