| Literature DB >> 2015900 |
K Maeda1, A Rösch, Y Maéda, H R Kalbitzer, A Wittinghofer.
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.Entities:
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Year: 1991 PMID： 2015900 DOI： 10.1016/0014-5793(91)80349-8
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124