Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase
about
Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymesPerspectives on electrostatics and conformational motions in enzyme catalysisSite-specific infrared probes of proteinsQuantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase.Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active siteProbing the Electrostatics of Active Site Microenvironments along the Catalytic Cycle for Escherichia coli Dihydrofolate ReductasePicosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changesMetal-ion effects on the polarization of metal-bound water and infrared vibrational modes of the coordinated metal center of Mycobacterium tuberculosis pyrazinamidase via quantum mechanical calculations.Site-specific measurement of water dynamics in the substrate pocket of ketosteroid isomerase using time-resolved vibrational spectroscopyValidation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophanSolvatochromism and the solvation structure of benzophenone.Electric Fields and Enzyme Catalysis.Measuring electrostatic fields in both hydrogen-bonding and non-hydrogen-bonding environments using carbonyl vibrational probes.Calculation of vibrational shifts of nitrile probes in the active site of ketosteroid isomerase upon ligand binding.BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Calculations of the electric fields in liquid solutions.Comment on "Transient Conformational Changes of Sensory Rhodopsin II Investigated by Vibrational Stark Effect Probes".Ionic effects on the proton transfer mechanism in aqueous solutions.Vibrational dynamics and solvatochromism of the label SCN in various solvents and hemoglobin by time dependent IR and 2D-IR spectroscopy.
P2860
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P2860
Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@ast
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@en
type
label
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@ast
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@en
prefLabel
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@ast
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@en
P2860
P356
P1476
Direct measurement of the prot ...... cycle in ketosteroid isomerase
@en
P2093
Kelly J Gaffney
Santosh Kumar Jha
P2860
P304
16612-16617
P356
10.1073/PNAS.1113874108
P407
P577
2011-09-26T00:00:00Z