Structural difference between two ATP-binding sites of heavy meromyosin revealed by the dynamic fluorescence quenching technique-Reference-Cited by-同舟云学术

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Structural difference between two ATP-binding sites of heavy meromyosin revealed by the dynamic fluorescence quenching technique

Published:1984-06 Issue:2 Volume:787 Page:113-121
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Miyata Hidetake,Asai Hiroshi

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference20 articles.

1. Heterogeneity in Enzymatic Sites of Heavy Meromyosin Shown by Measuring F-Actin-Inactivated Hydrolysis of β-Naphthyl Triphosphate1

2. Amphoteric Charge Distribution at the Enzymatic Site of 1,N6-Ethenoadenosine Triphosphate-Binding Heavy Meromyosin Determined by Dynamic Fluorescence Quenching1

3. Spectroscopic isolation of ES complexes of myosin subfragment-1 ATPase by fluorescence quenching

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Two Non-Identical Heads of Myosin Molecules;The Journal of Biochemistry;1986-01

2. Relationship between the ATPase Activity and the ATP-Induced Fluorescence Enhancement of SH-Modified Heavy Meromyosin during Its Fractional Inactivation by Vanadate plus ADP: Evidence for Heterogeneity in the Active Sites1;The Journal of Biochemistry;1985-06

3. Fluorescence Quenching: Theory and Applications;Topics in Fluorescence Spectroscopy

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