Journal of Applied Spectroscopy

, Volume 6, Issue 1, pp 49–50 | Cite as

A spectrofluorimetric study of the interaction of myosin with ATP

  • E. A. Burshtein


Formation of the enzymatically active rnyosin-ATP complex produces a reversible change in the fluorescence of the tryptophan residues, which may be interpreted in terms of a structural rearrangement causing the tryptophan to enter a more hydrophobic environment. Fluorescence is used to follow the kinetics of the formation and decomposition of the enzyme-substrate complex.


Analytical Chemistry Molecular Structure Tryptophan Structural Rearrangement Tryptophan Residue 
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Copyright information

© The Faraday Press, Inc. 1970

Authors and Affiliations

  • E. A. Burshtein

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