Half-stoichiometric trinitrophenylation of myosin subfragment 1 in the presence of pyrophosphate or adenosine diphosphate.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference35 articles.
1. Characterization of the ethenoadenosine diphosphate binding site of myosin subfragment. 1. Energetics of the equilibrium between two states of nucleotide.cntdot.S1 and vanadate-induced global conformation changes detected by energy transfer
2. Separation of SH-Modified Myosin Subfragment-1(A1) Isozyme into Two Distinct Equimolar Fractions by an Affinity Chromatography1
3. Intermediate oxygen exchange catalyzed by the actin-activated skeletal myosin adenosine triphosphatase
4. Effect of trinitrophenylation on myosin ATPase
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1. Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications;Chemical Reviews;2020-04-22
2. Peroxynitrite-mediated oxidative modifications of myosin and implications on structure and function;Free Radical Research;2010-09-06
3. Dynamic laser light scattering studies of the effects of pyrophosphate on cyclic motions of cross-bridges in isolated thick myofilaments fromLimulus striated muscle;Experientia;1994-09
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