Two-dimensional NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates
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P450cam Visits an Open Conformation in the Absence of Substrate ,Plasticity of Cytochrome P450 2B4 as Investigated by Hydrogen-Deuterium Exchange Mass Spectrometry and X-ray CrystallographyThe structure of CYP101D2 unveils a potential path for substrate entry into the active siteStructural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding siteMolecular dynamics of CYP2D6 polymorphisms in the absence and presence of a mechanism-based inactivator reveals changes in local flexibility and dominant substrate access channelsComputational prediction of metabolism: sites, products, SAR, P450 enzyme dynamics, and mechanismsHuman cytochrome P450 17A1 conformational selection: modulation by ligand and cytochrome b5.Structural features of cytochromes P450 and ligands that affect drug metabolism as revealed by X-ray crystallography and NMR.Three clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel.Enhancing the efficiency and regioselectivity of P450 oxidation catalysts by unnatural amino acid mutagenesis.Interactions of cytochrome P450s with their ligands.Active-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119.Dynamics and flexibility of human aromatase probed by FTIR and time resolved fluorescence spectroscopyAnalysis of cytochrome P450 CYP119 ligand-dependent conformational dynamics by two-dimensional NMR and X-ray crystallography.An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media.Using molecular dynamics to probe the structural basis for enhanced stability in thermal stable cytochromes P450.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Comparison of intrinsic dynamics of cytochrome p450 proteins using normal mode analysis.Advances in the Understanding of Protein-Protein Interactions in Drug Metabolizing Enzymes through the Use of Biophysical Techniques.The dynamics of camphor in the cytochrome P450 CYP101D2.Stochastic ensembles, conformationally adaptive teamwork, and enzymatic detoxification.
P2860
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P2860
Two-dimensional NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Two-dimensional NMR and all-at ...... idden conformational substates
@ast
Two-dimensional NMR and all-at ...... idden conformational substates
@en
type
label
Two-dimensional NMR and all-at ...... idden conformational substates
@ast
Two-dimensional NMR and all-at ...... idden conformational substates
@en
prefLabel
Two-dimensional NMR and all-at ...... idden conformational substates
@ast
Two-dimensional NMR and all-at ...... idden conformational substates
@en
P2093
P2860
P356
P1476
Two-dimensional NMR and all-at ...... idden conformational substates
@en
P2093
Paul R Ortiz de Montellano
Relly Brandman
Santhosh Sivaramakrishnan
P2860
P304
P356
10.1074/JBC.M109.087593
P407
P50
P577
2010-01-22T00:00:00Z