Dynamic personalities of proteins

The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity

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The Energy Landscapes and Motions of Proteins

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Attenuated T 2 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

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Dynamics of folded proteins

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Energy transfer: a spectroscopic ruler.

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The calculation of the potential of mean force using computer simulations

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Dynamics of ligand binding to myoglobin

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Accelerated molecular dynamics: A promising and efficient simulation method for biomolecules

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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

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The Catalytic Pathway of Cytochrome P450cam at Atomic Resolution

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A Perspective on Enzyme Catalysis

Benkovic, S. J., & Hammes‐Schiffer, S. (2003) · Science · doi:10.1126/science.1085515 · Cited by 1,281 · see citing works

Molecular Dynamics: Survey of Methods for Simulating the Activity of Proteins

Adcock, S. A., & McCammon, J. A. (2006) · Chemical Reviews · doi:10.1021/cr040426m · Cited by 1,279 · see citing works

Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

Frauenfelder, H., Petsko, G. A., & Tsernoglou, D. (1979) · Nature · doi:10.1038/280558a0 · Cited by 1,151 · see citing works

Dynamical transition of myoglobin revealed by inelastic neutron scattering

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Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

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A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Henzler‐Wildman, K. A., Lei, M., Thai, V., Kerns, S. J., Karplus, M., & Kern, D. (2007) · Nature · doi:10.1038/nature06407 · Cited by 1,067 · see citing works

Intrinsic dynamics of an enzyme underlies catalysis

Eisenmesser, E., Millet, Ó., Labeikovsky, W., Korzhnev, D., Wolf-Watz, M., Bosco, D. A., Skalicky, J., Kay, L., & Kern, D. (2005) · Nature · doi:10.1038/nature04105 · Cited by 1,057 · see citing works

Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex

Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032 · see citing works

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

Pervushin, K. V., Riek, R., Wider, G., & Kurt Wüthrich, A. (2021) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789811235795_0006 · Cited by 951 · see citing works

Protein folding funnels: a kinetic approach to the sequence-structure relationship.

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Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible

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Intrinsic motions along an enzymatic reaction trajectory

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NMR Characterization of the Dynamics of Biomacromolecules

Palmer, A. G. I. (2004) · Chemical Reviews · doi:10.1021/cr030413t · Cited by 889 · see citing works

Method for estimating the configurational entropy of macromolecules

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Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

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Protein states and proteinquakes.

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Gaussian Dynamics of Folded Proteins

Haliloǧlu, T., Bahar, İ., & Erman, B. (1997) · Physical Review Letters · doi:10.1103/physrevlett.79.3090 · Cited by 806 · see citing works

New Tools Provide New Insights in NMR Studies of Protein Dynamics

Mittermaier, A., & Kay, L. E. (2006) · Science · doi:10.1126/science.1124964 · Cited by 785 · see citing works

Enzyme Dynamics During Catalysis

Eisenmesser, E. Z., Bosco, D. A., Akke, M., & Kern, D. (2002) · Science · doi:10.1126/science.1066176 · Cited by 732 · see citing works

Calmodulin structure refined at 1.7 Å resolution

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Protein flexibility predictions using graph theory

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A Relaxation-Compensated Carr−Purcell−Meiboom−Gill Sequence for Characterizing Chemical Exchange by NMR Spectroscopy

Loria, J. P., Rance, M., & Palmer, A. G. I. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983961a · Cited by 695 · see citing works

Slaving: Solvent fluctuations dominate protein dynamics and functions

Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Parak, F. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212637899 · Cited by 677 · see citing works

Solvent viscosity and protein dynamics

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Conformational entropy in molecular recognition by proteins

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Solution structure of calcium-free calmodulin

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Folding funnels, binding funnels, and protein function

Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648 · see citing works

Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands

Noskov, S. Y., Bernèche, S., & Roux, B. (2004) · Nature · doi:10.1038/nature02943 · Cited by 598 · see citing works

Two-State Allosteric Behavior in a Single-Domain Signaling Protein

Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D. (2001) · Science · doi:10.1126/science.291.5512.2429 · Cited by 594 · see citing works

Molecular Motors: A Theorist's Perspective

Kolomeisky, A. B., & Fisher, M. E. (2006) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.58.032806.104532 · Cited by 561 · see citing works

4D ULTRAFAST ELECTRON DIFFRACTION, CRYSTALLOGRAPHY, AND MICROSCOPY

Zewail, A. H. (2006) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.57.032905.104748 · Cited by 549 · see citing works

Quantitative dynamics and binding studies of the 20S proteasome by NMR

Sprangers, R., & Kay, L. E. (2007) · Nature · doi:10.1038/nature05512 · Cited by 530 · see citing works

Single-Molecule Fluorescence Studies of Protein Folding and Conformational Dynamics

Michalet, X., Weiss, S., & Jäger, M. (2006) · Chemical Reviews · doi:10.1021/cr0404343 · Cited by 526 · see citing works

Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions

Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Young, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405573101 · Cited by 524 · see citing works

"New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding Simulations

Lazaridis, T., & Karplus, M. (1997) · Science · doi:10.1126/science.278.5345.1928 · Cited by 507 · see citing works

Slow Dynamics in Folded and Unfolded States of an SH3 Domain

Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., et al. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011300z · Cited by 506 · see citing works

Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

Wolf‐Watz, M., Thai, V., Henzler‐Wildman, K. A., Hadjipavlou, G., Eisenmesser, E. Z., & Kern, D. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb821 · Cited by 494 · see citing works

An NMR Perspective on Enzyme Dynamics

Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 460 · see citing works

Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding

Yang, D., & Kay, L. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0581 · Cited by 459 · see citing works

Solvent effects on protein motion and protein effects on solvent motion

Brooks, C. L., & Karplus, M. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90093-4 · Cited by 411 · see citing works

Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional Consequences

Jarymowycz, V. A., & Stone, M. J. (2006) · Chemical Reviews · doi:10.1021/cr040421p · Cited by 410 · see citing works

Hydrogen exchange and mass spectrometry: A historical perspective

Englander, S. W. (2006) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2006.06.006 · Cited by 405 · see citing works

Targeted Molecular Dynamics Simulation of Conformational Change-Application to the T ↔ R Transition in Insulin

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Protein-Folding Dynamics: Overview of Molecular Simulation Techniques

Scheraga, H. A., Khalili, M., & Liwo, A. (2006) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.58.032806.104614 · Cited by 398 · see citing works

Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase

Diez, M., Zimmermann, B., Börsch, M., König, M., Schweinberger, E., Steigmiller, S., Reuter, R., Felekyan, S., Kudryavtsev, V., Seidel, C. A. M., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb718 · Cited by 391 · see citing works

Protein Folding Thermodynamics and Dynamics: Where Physics, Chemistry, and Biology Meet

Shakhnovich, E. I. (2006) · Chemical Reviews · doi:10.1021/cr040425u · Cited by 372 · see citing works

NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9k

Akke, M., Brueschweiler, R., & Palmer, A. G. I. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00074a073 · Cited by 356 · see citing works

Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations

Paci, E., & Karplus, M. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2670 · Cited by 344 · see citing works

Magic-Angle Spinning Solid-State NMR Spectroscopy of the β1 Immunoglobulin Binding Domain of Protein G (GB1): 15N and13C Chemical Shift Assignments and Conformational Analysis

Franks, W. T., Zhou, D. H., Wylie, B. J., Money, B. G., Graesser, D. T., Schmidt, H. L. F., Sahota, G., & Rienstra, C. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044497e · Cited by 328 · see citing works

Nonequilibrium solvation effects on reaction rates for model SN2 reactions in water

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Single-molecule biophysics: at the interface of biology, physics and chemistry

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NMR studies of protein structure and dynamics

Kay, L. E. (2004) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2004.11.021 · Cited by 290 · see citing works

Dynamical Contributions to Enzyme Catalysis: Critical Tests of A Popular Hypothesis

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Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases

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A TROSY CPMG sequence for characterizing chemical exchange in large proteins

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Myoglobin: The hydrogen atom of biology and a paradigm of complexity

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Insights into the local residual entropy of proteins provided by NMR relaxation

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Quantitative NMR spectroscopy of supramolecular complexes: Dynamic side pores in ClpP are important for product release

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Ion selectivity in potassium channels

Noskov, S. Y., & Roux, B. (2006) · Biophysical Chemistry · doi:10.1016/j.bpc.2006.05.033 · Cited by 201 · see citing works

Constrained geometric simulation of diffusive motion in proteins

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Structural basis for endothelial nitric oxide synthase binding to calmodulin

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A Closed Compact Structure of Native Ca2+-Calmodulin

Fallon, J. L., & Quiocho, F. A. (2003) · Structure · doi:10.1016/j.str.2003.09.004 · Cited by 171 · see citing works

Picosecond time-resolved X-ray crystallography: probing protein function in real time

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Recent successes of the energy landscape theory of protein folding and function

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Advances in kinetic protein crystallography

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Conformational Flexibility of a Microcrystalline Globular Protein: Order Parameters by Solid-State NMR Spectroscopy

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Expanding the model: anisotropic displacement parameters in protein structure refinement

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Backbone dynamics and energetics of a Calmodulin domain mutant exchanging between closed and open conformations

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Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis

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Energetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding

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Direct NMR observation of a substrate protein bound to the chaperonin GroEL

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Protein folding and the organization of the protein topology universe

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Roles of classical dynamics and quantum dynamics on activated processes occurring in liquids

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Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High-Molecular-Weight Systems

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Structure of the Complex of Calmodulin with the Target Sequence of Calmodulin-Dependent Protein Kinase I: Studies of the Kinase Activation Mechanism

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Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy

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What Contributions to Protein Side-chain Dynamics are Probed by NMR Experiments? A Molecular Dynamics Simulation Analysis

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Energetics of target peptide recognition by calmodulin: A calorimetric study

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Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes

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Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel

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Temperature Dependence of the Internal Dynamics of a Calmodulin−Peptide Complex

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Transition Path Sampling Simulations of Biological Systems

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Quantitative 13C and 2H NMR Relaxation Studies of the 723-Residue Enzyme Malate Synthase G Reveal a Dynamic Binding Interface

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Calmodulin, Conformational States, and Calcium Signaling. A Single-Molecule Perspective

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Ultrafast catalytic processes in enzymes

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Protein Folding Pathways Studied by Pulsed- and Native-State Hydrogen Exchange

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Dual Effect of ATP in the Activation Mechanism of Brain Ca2+/Calmodulin-Dependent Protein Kinase II by Ca2+/Calmodulin

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Bridging Conformational Dynamics and Function Using Single-Molecule Spectroscopy

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The Molecular Basis of G Protein–Coupled Receptor Activation

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Global dynamics of proteins: bridging between structure and function

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Predicting multiple conformations via sequence clustering and AlphaFold2

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Protein activity regulation by conformational entropy

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Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

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Mapping allosteric communications within individual proteins

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Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics

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Multidomain structure and correlated dynamics determined by self-consistent FRET networks

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