Related Articles51V NMR study of vanadate binding to myosin and its subfragment 1.
Biochemistry. 1990 Sep 25;29(38):9091-6
Authors: Ringel I, Peyser YM, Muhlrad A
The binding of various forms of vanadate to myosin and myosin subfragment 1 (S-1) was studied by 51V NMR at increasing vanadate concentrations between 0.06 and 1.0 mM. The distribution of the various forms of vanadate in the solution depended on the total concentration of vanadate. At low concentrations, the predominant vanadate form was monomeric, while at high concentration, it was tetrameric. The presence of myosin or S-1 in the solution produced a significant broadening of the signal of each form of vanadate, indicating that all of them bind to the protein. Addition of ATP, which does not affect the 51V NMR spectra in the absence of proteins, causes their significant alteration in the presence of myosin or S-1. The changes, which include the broadening of the signal of the monomeric and the narrowing of the signal of the oligomeric vanadate forms, indicate that more monomeric and less oligomeric vanadate binds to the proteins in the presence than in the absence of ATP. Irradiation by near-UV light in the presence of vanadate cleaves S-1 at three specific sites--at 23, 31, and 74 kDa from the N-terminus. The cleavages at 23 and 31 kDa are specifically inhibited by the addition of ATP. The vanadate-associated photocleavage of S-1 also depends on the total concentration of vanadate; it is observed only when the concentration of vanadate is at least 0.2 mM. This was also the lowest concentration at which oligomeric vanadate was detected in the 51V NMR spectra. From the parallel concentration dependence of the photocleavage and the appearance of the tetrameric vanadate, it is concluded that photocleavage occurs only when tetrameric vanadate binds to S-1.
[NMR paper] Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosp
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
Related Articles Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
J Mol Biol. 2001 Dec 7;314(4):839-49
Authors: Ohki S, Eto M, Kariya E, Hayano T, Hayashi Y, Yazawa M, Brautigan D, Kainosho M
Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and...
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[NMR paper] NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
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Protein Sci. 1999 Aug;8(8):1711-3
Authors: Hannan JP, Whittaker SB, Davy SL, Kühlmann UC, Pommer AJ, Hemmings AM, James R, Kleanthous C, Moore GR
Ni2+ affinity columns are widely used for protein purification, but they carry the risk that Ni2+ ions may bind to the protein, either adventitiously or at a physiologically important site. Dialysis against ethylenediaminetetraacetic acid...
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[NMR paper] An NMR study of ligand binding by maltodextrin binding protein.
An NMR study of ligand binding by maltodextrin binding protein.
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Biochem Cell Biol. 1998;76(2-3):189-97
Authors: Gehring K, Zhang X, Hall J, Nikaido H, Wemmer DE
Proton NMR spectra of maltodextrin binding protein from Escherichia coli were used to monitor conformational changes that accompany ligand binding. Chemical shift changes associated with the binding of different maltodextrins to maltodextrin binding protein were studied using one-dimensional difference...
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[NMR paper] Interaction of a type II myosin with biological membranes studied by 2H solid state N
Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
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Biochemistry. 1998 Apr 21;37(16):5582-8
Authors: Arêas JA, Gröbner G, Glaubitz C, Watts A
Deuterium nuclear magnetic resonance spectroscopy (2H NMR) has been employed to investigate the interaction of lung type II myosin protein with neutral bilayers containing dimyristoylphosphatidylcholine (DMPC) as the only constituent and mixed bilayers containing...
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[NMR paper] Analysis of stress in the active site of myosin accompanied by conformational changes
Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy.
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Eur J Biochem. 1998 Mar 15;252(3):520-9
Authors: Maruta S, Henry GD, Ohki T, Kambara T, Sykes BD, Ikebe M
Myosin forms stable ternary complexes with ADP and the...
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[NMR paper] 13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
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J Biochem. 1994 Nov;116(5):1153-5
Authors: Kakuta Y, Hojo H, Aimoto S, Tanaka I, Hikichi K
The mobility of the DNA-binding arm of HU protein was studied by 13C-NMR spectroscopy. The correlation times tau c of Phe47C alpha in the body and Gly60C alpha in the arm of HU were determined for HU and HU-DNA complex. The value of tau c of Phe47C alpha is 2-4 times larger than that of Gly60C alpha...
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[NMR paper] 7Li NMR relaxation study of Li+ binding in human erythrocytes.
7Li NMR relaxation study of Li+ binding in human erythrocytes.
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Biochemistry. 1993 Dec 14;32(49):13490-8
Authors: Rong Q, Espanol M, Mota de Freitas D, Geraldes CF
We used 7Li NMR spin-lattice (T1) and spin-spin (T2) relaxation time measurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular 7Li NMR T2 relaxation value (0.30 +/- 0.03 s) was much smaller than the corresponding T1 value...
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[NMR paper] 19F NMR study of the myosin and tropomyosin binding sites on actin.
19F NMR study of the myosin and tropomyosin binding sites on actin.
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Biochemistry. 1990 Feb 6;29(5):1348-54
Authors: Barden JA, Phillips L
Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization . Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum...
51V NMR study of vanadate binding to myosin and its subfragment 1.
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