Key result
Photoaffinity labeling and 19F-NMR spectroscopy revealed variations in protein-nucleotide contacts at the nucleotide base among myosin ternary complexes, mimicking transient steps in the contractile cycle.
Population
Skeletal and smooth muscle myosin
Design
Preclinical
Authors
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Offers structural insights into myosin function; leaves open translation to human cardiac therapeutics.
The study reveals variations in protein-nucleotide contacts at the nucleotide base among myosin ternary complexes, providing insight into the transient steps of the contractile cycle.
Maruta et al. (1998) studied this question. Mant-2-N3-ADP and 19F-labeled ADP analogue was evaluated on Conformational differences in protein-nucleotide contact in the ATP-binding site. Photoaffinity labeling and 19F-NMR spectroscopy revealed variations in protein-nucleotide contacts at the nucleotide base among myosin ternary complexes, mimicking transient steps in the contractile cycle.
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