Conformational Changes in Myosin under ATP Hydrolysis
نویسندگان
چکیده
منابع مشابه
A FRET-Based Sensor Reveals Large ATP Hydrolysis–Induced Conformational Changes and Three Distinct States of the Molecular Motor Myosin
The molecular motor myosin is proposed to bind to actin and swing its light-chain binding region through a large angle to produce an approximately 10 nm step in motion coupled to changes in the nucleotide state at the active site. To date, however, direct dynamic measurements have largely failed to show changes of that magnitude. Here, we use a cysteine engineering approach to create a high res...
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The heat production during the ATP hydrolysis catalyzed by myosin subfragment 1 in 0.1 M KC1 containing 0.01 M MgClz and 0.02 M Tris/HCl (pH 7.8) at 23°C was followed using a microcalorimeter with an improved time resolution. The results indicate that: (a) the binding of ATP to Subfragment 1 is exothermic (AH = -90 kJ mol-‘, all the AH values are corrected for protonation heat of Tris). (b) The...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03669.x