title: Rabbit skeletal muscle myosin. Unfolded carboxyl-terminus and its role in molecular assembly.
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.
authors.affiliation: Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Maeda
authors.forename: A
authors.initials: A
authors.lastname: Rösch
authors.forename: Y
authors.initials: Y
authors.lastname: Maéda
authors.forename: H R
authors.initials: HR
authors.lastname: Kalbitzer
authors.forename: A
authors.initials: A
authors.lastname: Wittinghofer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005822:Genetic Vectors; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000737:chemistry / Q000235:genetics*; D015345:Oligonucleotide Probes; D011487:Protein Conformation; D011817:Rabbits; D012995:Solubility
chemical_list: D015345:Oligonucleotide Probes; D009218:Myosins