Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis.
about
Kinetics of peptide folding in lipid membranesFunctional and Structural Roles of the Cys14–Cys38 Disulfide of Bovine Pancreatic Trypsin InhibitorInvestigation of Catalytic Loop Structure, Dynamics, and Function Relationship of Yersinia Protein Tyrosine Phosphatase by Temperature-Jump Relaxation Spectroscopy and X-ray Structural DeterminationVersatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY)Physicochemical biology: conquered boundaries and new horizonsAnisotropic energy flow and allosteric ligand binding in albumin.The dynamical nature of enzymatic catalysis.Nanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.Spectroscopic studies of protein folding: linear and nonlinear methodsProbing the role of dynamics in hydride transfer catalyzed by lactate dehydrogenase.Protein dynamics from time resolved UV Raman spectroscopyLoop-tryptophan human purine nucleoside phosphorylase reveals submillisecond protein dynamics.Dynamic active-site protection by the M. tuberculosis protein tyrosine phosphatase PtpB lid domain.Measurement of circular dichroism dynamics in a nanosecond temperature-jump experiment.Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopyLoop residues and catalysis in OMP synthase.Temperature jump and fast photochemical oxidation probe submillisecond protein folding.Conformational heterogeneity within the Michaelis complex of lactate dehydrogenaseDissection of complex protein dynamics in human thioredoxinMechanism of Thermal Adaptation in the Lactate Dehydrogenases.Infrared spectroscopic discrimination between the loop and alpha-helices and determination of the loop diffusion kinetics by temperature-jump time-resolved infrared spectroscopy for cytochrome cSite-specific solvation of the photoexcited protochlorophyllide a in methanol: formation of the hydrogen-bonded intermediate state induced by hydrogen-bond strengtheningLigand-Dependent Conformational Dynamics of Dihydrofolate Reductase.On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase.Thermal-induced dissociation and unfolding of homodimeric DsbC revealed by temperature-jump time-resolved infrared spectra.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.Identification of two-step chemical mechanisms and determination of thermokinetic parameters using frequency responses to small temperature oscillations.Dissociation kinetics of the streptavidin-biotin interaction measured using direct electrospray ionization mass spectrometry analysis.Isotope-Labeled Aspartate Sidechain as a Non-Perturbing Infrared Probe: Application to Investigate the Dynamics of a Carboxylate Buried Inside a Protein.Coordination to lanthanide ions distorts binding site conformation in calmodulin.Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences.In Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function
P2860
Q26859563-E2E83499-EE91-42E0-A9FA-85E359B73733Q27651502-00F63C7B-E8B5-486D-A4F9-0BC9936A89E4Q27678944-4CDF96A6-C167-4CE1-8BB6-9BF5488BB52EQ28650940-DA17CF51-E6E1-4D46-ADD3-F7AEB32418D1Q28728669-D1C51C5C-197A-4D0B-ABD0-EF0AB2297A6DQ30358108-C6FF729A-B96A-41E5-A7FC-78B40D1BC878Q30370122-04E62D01-CC6A-4BB8-82C7-F8401F657AC8Q30388775-C0446E97-98A2-46B3-8AA3-1A6DEE7CEF71Q31042100-63B50FB8-28A5-4519-8433-5E42DF56B99AQ33335635-9D1844C5-0CBD-45B1-A192-A5008C6B75FFQ33349663-F33B2D89-98BD-4DFB-88D3-8EE4393C708BQ33405379-19AECC0A-275D-4FA4-A47E-633A84626048Q33806251-0BE9D554-7032-43CB-A72A-40B78E5CAE22Q33922098-B514F200-931E-48FF-813C-CDCD9D90A75BQ34202597-0A5B7FC1-D3A4-47A0-B1E5-96831E0AE044Q34270718-87D3D583-AD8F-4DEC-9FD4-96857DE14232Q34287246-E869FE52-3AB7-4B8D-8039-5B11B51B3160Q35036392-B4BEE0C8-EC4D-42BC-97B0-662C49A97BE1Q35720786-EE6F8967-F837-4010-9DE0-576FAE1D84B4Q35837731-0C3F1567-0073-4FE3-B1AA-B92725EBC9DEQ36008707-874D5664-20D2-4457-9E29-E0209C57204FQ36259565-A9DE36C2-8C95-4B61-98D0-51E430EEDC89Q36725885-9F648401-2F91-420B-99D1-D904ABDB721DQ36737129-6D389658-79D3-4824-84F3-1924A2B0DD9FQ37418764-44B8D017-5138-4965-B14A-E8C9F21FECF6Q38287400-7240E2E3-B5A6-4AA6-9B9E-B6D2B2F6E906Q39894991-24CBE13E-36F8-4933-BC34-1FBB80FB1B1FQ44828715-D9B32B87-64B5-4F51-AC1A-C49BE1797F08Q45740523-618E85B7-46AB-4E1E-B445-1F3E73697E34Q47650790-ED08CF14-AE73-49A0-AB7B-8FA4D116E541Q52353920-69A1993B-8B52-44AE-92F8-B7C75056722DQ53395592-343E7F49-3F46-484E-B4A5-DDA276E2178EQ58042970-04A3BA7A-4D73-4254-AC46-7D5C2242BBBD
P2860
Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@ast
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@en
type
label
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@ast
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@en
prefLabel
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@ast
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@en
P356
P1433
P1476
Advances in time-resolved appr ...... nature of enzymatic catalysis.
@en
P2093
R Brian Dyer
Robert Callender
P304
P356
10.1021/CR050284B
P577
2006-08-01T00:00:00Z