Protein dynamics and function from solution state NMR spectroscopy

scientific article published on January 2016

Protein dynamics and function from solution state NMR spectroscopy is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1017/S0033583516000019
P698PubMed publication ID27088887

P2093author name stringMagnus Wolf-Watz
Michael Kovermann
Per Rogne
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Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMRQ37010689
A unified model of protein dynamics.Q37112478
Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulinQ37114735
Protein-protein interaction and quaternary structureQ37277360
Role of conformational entropy in the activity and regulation of the catalytic subunit of protein kinase A.Q37290105
Conformational selection or induced fit: a flux description of reaction mechanismQ37310586
Residual dipolar couplings as a tool to study molecular recognition of ubiquitin.Q37330478
Dynamically driven protein allostery.Q37376854
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain foldingQ37564668
Alanine scan of core positions in ubiquitin reveals links between dynamics, stability, and functionQ37633562
Using NMR to study fast dynamics in proteins: methods and applicationsQ37798994
Dynamics in electron transfer protein complexesQ37847241
Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.Q38044412
Describing intrinsically disordered proteins at atomic resolution by NMR.Q38094877
Advances in solid-state relaxation methodology for probing site-specific protein dynamicsQ38102033
Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopyQ38203952
Application of isothermal titration calorimetry for characterizing thermodynamic parameters of biomolecular interactions: peptide self-assembly and protein adsorption case studiesQ38240746
Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopyQ38300057
Conformational entropy changes upon lactose binding to the carbohydrate recognition domain of galectin-3.Q38351866
Spatially organized aggregation of misfolded proteins as cellular stress defense strategyQ38355473
NMR chemical exchange as a probe for ligand-binding kinetics in a theophylline-binding RNA aptamer.Q38355608
Bio-inspired design and potential biomedical applications of a novel class of high-affinity peptides.Q55462323
Der experimentelle Nachweis der Richtungsquantelung im MagnetfeldQ55954032
XXXII. On the influence of magnetism on the nature of the light emitted by a substanceQ56627700
Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole−Dipole Couplings in High-Resolution Biomolecular NMRQ56770089
Erratum: The role of dynamic conformational ensembles in biomolecular recognitionQ57078201
Measurement of intrinsic exchange rates of amide protons in a 15N-labeled peptideQ57078264
Magnetic Field Dependence of Nitrogen−ProtonJSplittings in15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar CouplingQ57080250
Side-Chain Orientation and Hydrogen-Bonding Imprint Supra-τc Motion on the Protein Backbone of UbiquitinQ57207980
Model-Free Analysis of Protein Backbone Motion from Residual Dipolar CouplingsQ57207998
Model-Free Approach to the Dynamic Interpretation of Residual Dipolar Couplings in Globular ProteinsQ57208003
UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz RatesQ57896537
SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few SecondsQ57896548
Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of SecondsQ57896552
Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteinsQ57904891
The Static Magnetic Field Dependence of Chemical Exchange Linebroadening Defines the NMR Chemical Shift Time ScaleQ57962655
Disorder-order folding transitions underlie catalysis in the helicase motor of SecAQ57976550
Conformational Dynamics and Molecular Recognition: Backbone Dynamics of the Estrogen Receptor DNA-binding DomainQ58008696
Backbone Dynamics ofEscherichia coliAdenylate Kinase at the Extreme Stages of the Catalytic Cycle Studied by15N NMR Relaxation†Q58406877
Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar CouplingsQ58484319
Quantitative dynamics and binding studies of the 20S proteasome by NMRQ59082478
Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do?Q59102877
Basis of Substrate Binding by the Chaperonin GroEL†Q59600026
Using Xplor–NIH for NMR molecular structure determinationQ60680250
Protein dynamics studied by rotating frame 15N spin relaxation times.Q64898708
Spin labeling of proteinsQ69362293
Kinetic studies on turtle pancreatic ribonuclease: a comparative study of the base specificities of the B2 and P0 sites of bovine pancreatic ribonuclease A and turtle pancreatic ribonucleaseQ69613686
Allostery without conformational change. A plausible modelQ70806307
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecBQ70923958
Rapid, electrostatically assisted association of proteinsQ71031198
Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognitionQ71624169
Following protein folding in real time using NMR spectroscopyQ71726951
Structural dynamics in an electron-transfer complexQ72012698
Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for functionQ73047075
Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approachQ73161333
Increased protein backbone conformational entropy upon hydrophobic ligand bindingQ73227017
Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labelsQ73335302
Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structuresQ73335305
Two-state allosteric behavior in a single-domain signaling proteinQ73662809
De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracyQ73825206
NMR relaxation studies of the role of conformational entropy in protein stability and ligand bindingQ73881230
1H/15N HSQC NMR studies of ligand carboxylate group interactions with arginine residues in complexes of brodimoprim analogues and Lactobacillus casei dihydrofolate reductaseQ74456833
Protein dynamics from NMRQ74779717
Heat does not come in different colours: entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactionsQ77530446
Potent inhibition of mammalian ribonucleases by 3', 5'-pyrophosphate-linked nucleotidesQ77754787
Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNAQ77928344
Influence of the fluctuations of the alignment tensor on the analysis of the structure and dynamics of proteins using residual dipolar couplingsQ79926586
NMR characterization of the dynamics of biomacromoleculesQ80435130
P304page(s)e6
P577publication date2016-01-01
P1433published inQuarterly Reviews of BiophysicsQ2361372
P1476titleProtein dynamics and function from solution state NMR spectroscopy
P478volume49

Reverse relations

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