scholarly article | Q13442814 |
P50 | author | Lewis E. Kay | Q29046014 |
P2093 | author name string | Andrew J Baldwin | |
P2860 | cites work | Relaxation Processes in a System of Two Spins | Q21651547 |
Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy | Q24311367 | ||
A consensus view of protein dynamics | Q24682188 | ||
Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments | Q27355457 | ||
Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR | Q27648890 | ||
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution | Q27650851 | ||
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding | Q27651198 | ||
Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy | Q27651564 | ||
Multiple conformational changes in enzyme catalysis | Q28206522 | ||
Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis | Q28239049 | ||
Molecular dynamics and protein function | Q28248486 | ||
Dynamics of folded proteins | Q28287584 | ||
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease | Q29547582 | ||
Intrinsic dynamics of an enzyme underlies catalysis | Q29616406 | ||
The dynamic energy landscape of dihydrofolate reductase catalysis | Q29616409 | ||
Dynamic personalities of proteins | Q29616723 | ||
Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy | Q30157066 | ||
Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy | Q30157745 | ||
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 spectroscopy | Q30159636 | ||
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states | Q30159675 | ||
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. | Q30163903 | ||
Slow Dynamics in Folded and Unfolded States of an SH3 Domain | Q30167790 | ||
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 | ||
Studying excited states of proteins by NMR spectroscopy. | Q30329160 | ||
Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. | Q30349857 | ||
Protein folding and misfolding: mechanism and principles. | Q30368801 | ||
Polymer principles in protein structure and stability. | Q30371172 | ||
Direct observation of the dynamic process underlying allosteric signal transmission. | Q30374830 | ||
Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments | Q44173306 | ||
Direct Observation of Protein−Ligand Interaction Kinetics | Q44592422 | ||
Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network | Q44795584 | ||
Millisecond protein folding studied by NMR spectroscopy | Q45276869 | ||
Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy | Q46428875 | ||
Multistate folding of the villin headpiece domain | Q46842230 | ||
Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems | Q47386308 | ||
An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562. | Q51510708 | ||
Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins | Q58045305 | ||
A microscopic view of chemical exchange: Monte Carlo simulation of molecular association | Q58428553 | ||
Nature of Forces between Large Molecules of Biological Interest* | Q59063408 | ||
Quantitative dynamics and binding studies of the 20S proteasome by NMR | Q59082478 | ||
Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? | Q59102877 | ||
Dynamics of ligand binding to myoglobin | Q67337334 | ||
Internal motion of proteins: nuclear magnetic resonance measurements and dynamic simulations | Q69647559 | ||
An x-ray study of azide methaemoglobin | Q72922745 | ||
Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function | Q73047075 | ||
Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach | Q73161333 | ||
Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions | Q73612009 | ||
Remarkably slow folding of a small protein | Q73626506 | ||
MECHANISM OF ENZYME CATALYSIS | Q77061011 | ||
Evidence for flexibility in the function of ribonuclease A | Q78056538 | ||
Probing structure in invisible protein states with anisotropic NMR chemical shifts | Q80653432 | ||
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 spectroscopy | Q80774504 | ||
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 spectroscopy | Q81403738 | ||
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states | Q81510160 | ||
Protein dynamism and evolvability. | Q30376087 | ||
Analysis of slow interdomain motion of macromolecules using NMR relaxation data | Q30656510 | ||
Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation | Q30932059 | ||
Sub-microsecond protein folding | Q33241430 | ||
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 enhancement | Q33595258 | ||
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 units | Q33935275 | ||
Protein dynamics from NMR. | Q34019517 | ||
Enzyme dynamics during catalysis | Q34115429 | ||
Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release | Q34133375 | ||
Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli | Q34173585 | ||
Spin glasses and the statistical mechanics of protein folding | Q34358450 | ||
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 perspective | Q34604753 | ||
Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex | Q35033085 | ||
The mechanism of rate-limiting motions in enzyme function. | Q35901179 | ||
Measurement of bond vector orientations in invisible excited states of proteins | Q36276828 | ||
Dynamic requirements for a functional protein hinge | Q36388178 | ||
Recent successes of the energy landscape theory of protein folding and function | Q36577998 | ||
Tailoring relaxation dispersion experiments for fast-associating protein complexes | Q36871716 | ||
On the relationship between folding and chemical landscapes in enzyme catalysis | Q36893577 | ||
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis | Q36924776 | ||
Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding | Q37084781 | ||
From the first protein structures to our current knowledge of protein folding: delights and scepticisms | Q37199653 | ||
Sending signals dynamically | Q37440289 | ||
An enzymatic molten globule: efficient coupling of folding and catalysis. | Q37511760 | ||
A 21st century revisionist's view at a turning point in enzymology | Q39961656 | ||
Mechanism of coupled folding and binding of an intrinsically disordered protein | Q40210194 | ||
Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobility | Q40323066 | ||
Complete tyrosine assignments in the high field proton nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitor | Q40340785 | ||
Investigation of protein motions via relaxation measurements | Q40576278 | ||
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 motions | Q41902515 | ||
Protein folding intermediates: native-state hydrogen exchange | Q42322493 | ||
Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair | Q43016326 | ||
P433 | issue | 11 | |
P921 | main subject | spectroscopy | Q483666 |
NMR spectroscopy | Q10359898 | ||
P304 | page(s) | 808-814 | |
P577 | publication date | 2009-11-01 | |
P13046 | publication type of scholarly work | review article | Q7318358 |
P1433 | published in | Nature Chemical Biology | Q904026 |
P1476 | title | NMR spectroscopy brings invisible protein states into focus | |
P478 | volume | 5 |
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Q38706821 | A Secondary Structural Element in a Wide Range of Fucosylated Glycoepitopes. |
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Q27664400 | A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution |
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Q38113523 | A personal perspective on chemistry-driven RNA research. |
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