Pages that link to "Q37267240"

The following pages link to Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis (Q37267240):

Displaying 41 items.

• SPARTA : a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network (Q24615699) (← links)
• NMR Methods to Study Dynamic Allostery (Q26766518) (← links)
• Allosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic Core (Q27678036) (← links)
• Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation (Q27681926) (← links)
• Equilibrium transitions between side-chain conformations in leucine and isoleucine. (Q30375057) (← links)
• NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination. (Q30385001) (← links)
• Structure-based prediction of methyl chemical shifts in proteins (Q30404690) (← links)
• Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered (Q30415349) (← links)
• Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus (Q33452730) (← links)
• Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance (Q33757683) (← links)
• Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts (Q33762885) (← links)
• Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements (Q33763065) (← links)
• Interpreting protein chemical shift data (Q33795387) (← links)
• Accurate measurement of methyl 13C chemical shifts by solid-state NMR for the determination of protein side chain conformation: the influenza a M2 transmembrane peptide as an example (Q33850192) (← links)
• Dynamic multidrug recognition by multidrug transcriptional repressor LmrR. (Q34531084) (← links)
• Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings (Q36333871) (← links)
• Improved chemical shift prediction by Rosetta conformational sampling (Q36356953) (← links)
• Metal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556 (Q36368801) (← links)
• Solid-state NMR study reveals collagen I structural modifications of amino acid side chains upon fibrillogenesis (Q36685136) (← links)
• Efficacy of the β₂-adrenergic receptor is determined by conformational equilibrium in the transmembrane region (Q36855917) (← links)
• Solution characterization of [methyl-(13)C]methionine HIV-1 reverse transcriptase by NMR spectroscopy (Q37252481) (← links)
• Side chain conformational averaging in human dihydrofolate reductase (Q38736537) (← links)
• Ab initio calculations of possible γ-gauche effects in the ¹³C-NMR for methine and carbonyl carbons in precise polyethylene acrylic acid copolymers. (Q39375426) (← links)
• Recent developments in solution nuclear magnetic resonance (NMR)-based molecular biology. (Q39393023) (← links)
• Mechanisms of allosteric gene regulation by NMR quantification of microsecond-millisecond protein dynamics (Q40401695) (← links)
• Conformational dependence of 13C shielding and coupling constants for methionine methyl groups (Q41080363) (← links)
• The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts (Q42170387) (← links)
• The application of tailor-made force fields and molecular dynamics for NMR crystallography: a case study of free base cocaine. (Q42319283) (← links)
• Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses. (Q42320264) (← links)
• Metal Ion Binding at the Catalytic Site Induces Widely Distributed Changes in a Sequence Specific Protein-DNA Complex (Q43110195) (← links)
• Determining Valine Side-Chain Rotamer Conformations in Proteins from Methyl 13C Chemical Shifts: Application to the 360 kDa Half-Proteasome (Q43631537) (← links)
• Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures. (Q45960129) (← links)
• Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2. (Q47797625) (← links)
• Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR. (Q48240503) (← links)
• A new model for mapping the peptide backbone: predicting proton chemical shifts in proteins. (Q51723900) (← links)
• Using Side-Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures (Q57678604) (← links)
• Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion (Q57896502) (← links)
• GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures (Q58568628) (← links)
• A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins (Q83973860) (← links)
• Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis (Q89149253) (← links)
• Chemical shift-based methods in NMR structure determination (Q91704782) (← links)