Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins. - Wikidata - wikimedia - TriplyDB

Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.

Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.

http://www.wikidata.org/entity/Q36216432

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Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks Fine-tuning multiprotein complexes using small molecules Structure of a Double Transmembrane Fragment of a G-Protein-Coupled Receptor in Micelles A Mechanism for the Auto-inhibition of Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) Channel Opening and Its Relief by cAMP Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR Intrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistance (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.FAST-NMR: functional annotation screening technology using NMR spectroscopy Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy.Structure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2 Dynamic Interaction of Hsp90 with Its Client Protein p53.The quiet renaissance of protein nuclear magnetic resonance.Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent The fungal natural product azaphilone-9 binds to HuR and inhibits HuR-RNA interaction in vitro.Structure elucidation of dimeric transmembrane domains of bitopic proteins Dynamics on multiple timescales in the RNA-directed RNA polymerase from the cystovirus phi6 FLAMEnGO 2.0: an enhanced fuzzy logic algorithm for structure-based assignment of methyl group resonances.Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.Toward a predictive understanding of slow methyl group dynamics in proteins Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps.Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin NMR distinction of single- and multiple-mode binding of small-molecule protein ligands.In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy.Accessing ns-micros side chain dynamics in ubiquitin with methyl RDCs.Optimized bacterial expression and purification of the c-Src catalytic domain for solution NMR studies.NMR reveals novel mechanisms of protein activity regulation.The dynamic duo: combining NMR and small angle scattering in structural biology.NMR studies of dynamic biomolecular conformational ensembles.Solution NMR Spectroscopy in Target-Based Drug Discovery.A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT.Internal motions prime cIAP1 for rapid activation.Slow conformational dynamics in the cystoviral RNA-directed RNA polymerase P2: influence of substrate nucleotides and template RNA.The HIV-1 p66 homodimeric RT exhibits different conformations in the binding-competent and -incompetent NNRTI site.An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.An efficient on-column expressed protein ligation strategy: application to segmental triple labeling of human apolipoprotein E3.Site-selective 13C labeling of histidine and tryptophan using ribose.The rhodopsin-arrestin-1 interaction in bicelles.Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

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P2860

Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.

http://www.wikidata.org/entity/Q36216432

description

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Vitali Tugarinov

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P2860

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis

Structure of theEscherichia colimalate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution

Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

The glyoxylate cycle is required for fungal virulence

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1567-1577

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10.1002/CBIC.200500110

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9

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6

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