Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy
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Physicochemical Properties of Ion Pairs of Biological MacromoleculesMolecular sled is an eleven-amino acid vehicle facilitating biochemical interactions via sliding components along DNA.Stereospecific Effects of Oxygen-to-Sulfur Substitution in DNA Phosphate on Ion Pair Dynamics and Protein-DNA AffinityNMR Spectroscopic Characterization of Charge Assisted Strong Hydrogen Bonds in Brønsted Acid CatalysisDynamic Equilibria of Short-Range Electrostatic Interactions at Molecular Interfaces of Protein-DNA Complexes.Residence Times of Molecular Complexes in Solution from NMR Data of Intermolecular Hydrogen-Bond Scalar CouplingPositive and negative impacts of nonspecific sites during target location by a sequence-specific DNA-binding protein: origin of the optimal search at physiological ionic strength.Effective strategy to assign ¹H- ¹⁵N heteronuclear correlation NMR signals from lysine side-chain NH3₃⁺ groups of proteins at low temperature.A chemical approach for site-specific identification of NMR signals from protein side-chain NH₃⁺ groups forming intermolecular ion pairs in protein-nucleic acid complexesEntropic Enhancement of Protein-DNA Affinity by Oxygen-to-Sulfur Substitution in DNA Phosphate.Balancing between affinity and speed in target DNA search by zinc-finger proteins via modulation of dynamic conformational ensembleChanges in conformational dynamics of basic side chains upon protein-DNA association.Dynamics and recognition within a protein-DNA complex: a molecular dynamics study of the SKN-1/DNA interaction.A Unique and Simple Approach to Improve Sensitivity in 15N-NMR Relaxation Measurements for NH₃⁺ Groups: Application to a Protein-DNA Complex.NMR Scalar Couplings across Intermolecular Hydrogen Bonds between Zinc-Finger Histidine Side Chains and DNA Phosphate Groups.Protein-DNA interfaces: a molecular dynamics analysis of time-dependent recognition processes for three transcription factors.Conformational Dynamics and the Binding of Specific and Nonspecific DNA by the Autoinhibited Transcription Factor Ets-1Entropy redistribution controls allostery in a metalloregulatory protein.pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.Microscopic understanding of the conformational features of a protein-DNA complex.Internal Motions of Basic Side Chains of the Antennapedia Homeodomain in the Free and DNA-Bound States.Asymmetric breathing motions of nucleosomal DNA and the role of histone tails.Wing 1 of protein HOP2 is as important as helix 3 in DNA binding by MD simulation.Protein-ligand (un)binding kinetics as a new paradigm for drug discovery at the crossroad between experiments and modellingImpact of two-bond N-N scalar couplings on N transverse relaxation measurements for arginine side chains of proteins
P2860
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P2860
Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 25 February 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Direct observation of the ion- ...... interface by NMR spectroscopy
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Direct observation of the ion- ...... interface by NMR spectroscopy.
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type
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Direct observation of the ion- ...... interface by NMR spectroscopy
@en
Direct observation of the ion- ...... interface by NMR spectroscopy.
@nl
prefLabel
Direct observation of the ion- ...... interface by NMR spectroscopy
@en
Direct observation of the ion- ...... interface by NMR spectroscopy.
@nl
P2093
P2860
P356
P1476
Direct observation of the ion- ...... interface by NMR spectroscopy
@en
P2093
Alexandre Esadze
David G Gorenstein
Junji Iwahara
Kurtis M Anderson
Mariappan Manoharan
Rafael Brüschweiler
P2860
P304
P356
10.1021/JA312314B
P407
P577
2013-02-25T00:00:00Z