Related ArticlesNMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide.
Biochim Biophys Acta. 1998 Nov 8;1442(2-3):137-47
Authors: van Lieshout E, Hemminga MA
To obtain a better understanding of the electrostatic nature of protein-nucleic acid interactions, we have investigated the interaction of a double-stranded decamer d(GGAAATTTCC)2 with a synthetic arginine and lysine-rich pentacosapeptide (Pep25), using NMR and optical spectroscopy. The chemical shift data of the decamer under various experimental conditions show that the binding of Pep25 changes the conformation of the decamer in a different way, as compared to the conformational changes induced by a variation in temperature or ionic strength. The chemical shift results are interpreted in terms of ring current effects that emerge into a model for the conformational change, in which the double-stranded helix of the decamer undergoes a decrease of twist and rise to accommodate Pep25. The binding results indicate that the positively charged arginine and lysine side chains of Pep25 not only have a stabilising electrostatic interaction with the negatively charged backbone phosphates of d(GGAAATTTCC)2, but also that a stabilisation of the base pairs of d(GGAAATTTCC)2 by Pep25 takes place.
[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
J Magn Reson. 2005 Jul;175(1):158-62
Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ
Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...
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[NMR paper] Dissecting structural and electrostatic interactions of charged groups in alpha-sarci
Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
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Biochemistry. 2003 Nov 18;42(45):13122-33
Authors: García-Mayoral MF, Pérez-Cañadillas JM, Santoro J, Ibarra-Molero B, Sanchez-Ruiz JM, Lacadena J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The cytotoxic ribonuclease...
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[NMR paper] Energetics by NMR: site-specific binding in a positively cooperative system.
Energetics by NMR: site-specific binding in a positively cooperative system.
Related Articles Energetics by NMR: site-specific binding in a positively cooperative system.
Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1847-52
Authors: Tochtrop GP, Richter K, Tang C, Toner JJ, Covey DF, Cistola DP
Proteins with multiple binding sites exhibit a complex behavior that depends on the intrinsic affinities for each site and the energetic communication between the sites. The contributions from intrinsic affinity and cooperativity are difficult to...
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11-24-2010 08:49 PM
[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.
Related Articles NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
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.
Related Articles An NMR study of ligand binding by maltodextrin binding protein.
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] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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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...
NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide
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