Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H−15N NMR spectroscopy.
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Physicochemical Properties of Ion Pairs of Biological MacromoleculesSolution structure of lysine-free (K0) ubiquitinStereospecific Effects of Oxygen-to-Sulfur Substitution in DNA Phosphate on Ion Pair Dynamics and Protein-DNA AffinityCHARMM36 all-atom additive protein force field: validation based on comparison to NMR dataDynamic Equilibria of Short-Range Electrostatic Interactions at Molecular Interfaces of Protein-DNA Complexes.Chemical exchange in biomacromolecules: past, present, and future.Effective strategy to assign ¹H- ¹⁵N heteronuclear correlation NMR signals from lysine side-chain NH3₃⁺ groups of proteins at low temperature.Toward a predictive understanding of slow methyl group dynamics in proteinsA 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.Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins.Protein lysine-Nζ alkylation and O-phosphorylation mediated by DTT-generated reactive oxygen species.Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopyChanges 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.A structural bioinformatics investigation on protein-DNA complexes delineates their modes of interaction.Protein-DNA interfaces: a molecular dynamics analysis of time-dependent recognition processes for three transcription factors.Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H.Measurement of 15N longitudinal relaxation rates in 15NH4+ spin systems to characterise rotational correlation times and chemical exchange.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.Internal Motions of Basic Side Chains of the Antennapedia Homeodomain in the Free and DNA-Bound States.Wing 1 of protein HOP2 is as important as helix 3 in DNA binding by MD simulation.Hydration of the Carboxylate Group in Anti-Inflammatory Drugs: ATR-IR and Computational Studies of Aqueous Solution of Sodium Diclofenac.Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groupsLyophilised protein dynamics: more than just methyls?
P2860
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P2860
Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H−15N NMR spectroscopy.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@en
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@nl
type
label
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@en
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@nl
prefLabel
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@en
Dynamics of lysine side-chain ...... clear 1H−15N NMR spectroscopy.
@nl
P2093
P356
P1476
Dynamics of lysine side-chain ...... uclear 1H−15N NMR spectroscopy
@en
P2093
Alexandre Esadze
Rafael Brüschweiler
Tianzhi Wang
P304
P356
10.1021/JA107847D
P407
P577
2011-02-01T00:00:00Z