NMR spectroscopy brings invisible protein states into focus

scientific article

NMR spectroscopy brings invisible protein states into focus is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1038/NCHEMBIO.238
P698PubMed publication ID19841630
P5875ResearchGate publication ID38022669

P50authorLewis E. KayQ29046014
P2093author name stringAndrew J Baldwin
P2860cites workRelaxation Processes in a System of Two SpinsQ21651547
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Multiple conformational changes in enzyme catalysisQ28206522
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Molecular dynamics and protein functionQ28248486
Dynamics of folded proteinsQ28287584
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Intrinsic dynamics of an enzyme underlies catalysisQ29616406
The dynamic energy landscape of dihydrofolate reductase catalysisQ29616409
Dynamic personalities of proteinsQ29616723
Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopyQ30157066
Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopyQ30157745
Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopyQ30159636
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate statesQ30159675
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Q30163903
Slow Dynamics in Folded and Unfolded States of an SH3 DomainQ30167790
The folding kinetics and thermodynamics of the Fyn-SH3 domain.Q30176267
Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.Q30193714
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Millisecond protein folding studied by NMR spectroscopyQ45276869
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Nature of Forces between Large Molecules of Biological Interest*Q59063408
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
Dynamics of ligand binding to myoglobinQ67337334
Internal motion of proteins: nuclear magnetic resonance measurements and dynamic simulationsQ69647559
An x-ray study of azide methaemoglobinQ72922745
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
Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutionsQ73612009
Remarkably slow folding of a small proteinQ73626506
MECHANISM OF ENZYME CATALYSISQ77061011
Evidence for flexibility in the function of ribonuclease AQ78056538
Probing structure in invisible protein states with anisotropic NMR chemical shiftsQ80653432
The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopyQ80774504
Quantifying two-bond 1HN-13CO and one-bond 1H(alpha)-13C(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopyQ81403738
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein statesQ81510160
Protein dynamism and evolvability.Q30376087
Analysis of slow interdomain motion of macromolecules using NMR relaxation dataQ30656510
Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformationQ30932059
Sub-microsecond protein foldingQ33241430
Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.Q33559311
Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancementQ33595258
Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Q33671554
Protein folding: the stepwise assembly of foldon unitsQ33935275
Protein dynamics from NMR.Q34019517
Enzyme dynamics during catalysisQ34115429
Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product releaseQ34133375
Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coliQ34173585
Spin glasses and the statistical mechanics of protein foldingQ34358450
The depth of chemical time and the power of enzymes as catalysts.Q34465289
Detecting transient intermediates in macromolecular binding by paramagnetic NMR.Q34518214
Visualization of transient encounter complexes in protein-protein association.Q34575140
Complexity and simplicity of ligand-macromolecule interactions: the energy landscape perspectiveQ34604753
Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complexQ35033085
The mechanism of rate-limiting motions in enzyme function.Q35901179
Measurement of bond vector orientations in invisible excited states of proteinsQ36276828
Dynamic requirements for a functional protein hingeQ36388178
Recent successes of the energy landscape theory of protein folding and functionQ36577998
Tailoring relaxation dispersion experiments for fast-associating protein complexesQ36871716
On the relationship between folding and chemical landscapes in enzyme catalysisQ36893577
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysisQ36924776
Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein foldingQ37084781
From the first protein structures to our current knowledge of protein folding: delights and scepticismsQ37199653
Sending signals dynamicallyQ37440289
An enzymatic molten globule: efficient coupling of folding and catalysis.Q37511760
A 21st century revisionist's view at a turning point in enzymologyQ39961656
Mechanism of coupled folding and binding of an intrinsically disordered proteinQ40210194
Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobilityQ40323066
Complete tyrosine assignments in the high field proton nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitorQ40340785
Investigation of protein motions via relaxation measurementsQ40576278
NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7.Q41837313
The spectrum of biomolecular states and motionsQ41902515
Protein folding intermediates: native-state hydrogen exchangeQ42322493
Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pairQ43016326
P433issue11
P921main subjectspectroscopyQ483666
NMR spectroscopyQ10359898
P304page(s)808-814
P577publication date2009-11-01
P13046publication type of scholarly workreview articleQ7318358
P1433published inNature Chemical BiologyQ904026
P1476titleNMR spectroscopy brings invisible protein states into focus
P478volume5

Reverse relations

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