Studying the role of protein dynamics in an SN2 enzyme reaction using free-energy surfaces and solvent coordinates.
about
Understanding DNA under oxidative stress and sensitization: the role of molecular modelingProbing the Electrostatics of Active Site Microenvironments along the Catalytic Cycle for Escherichia coli Dihydrofolate ReductaseThe importance of ensemble averaging in enzyme kineticsPerspective: Defining and quantifying the role of dynamics in enzyme catalysisComparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.The role of dimer asymmetry and protomer dynamics in enzyme catalysis.Computing the Free Energy Barriers for Less by Sampling with a Coarse Reference Potential while Retaining Accuracy of the Target Fine ModelTransition state theory for enzyme kinetics.Another Look at the Mechanisms of Hydride Transfer Enzymes with Quantum and Classical Transition Path Sampling.Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase.Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation.Quantifying the limits of transition state theory in enzymatic catalysis.Revealing the Origin of the Efficiency of the De Novo Designed Kemp Eliminase HG-3.17 by Comparison with the Former Developed HG-3.Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.
P2860
Q26799860-CCC1A93B-2084-48A0-8980-8DD066B4F8A5Q27684485-1B85982B-34E6-4FB4-8B63-85E6DEE68D87Q28081632-1980BD10-513A-415F-905A-3BF409FB3B02Q28834243-EDA85D7D-32B5-494B-AE07-E821BC7B9D5EQ30379469-46576027-AD7C-49BC-B10B-879C91FD6F04Q31155485-4CF9363C-C3CC-4353-9D99-2E6318A732D3Q34044954-3472D4E6-2DBD-451F-AEC9-E3B9E1F684F7Q36012016-DB19A410-2660-48F2-86FA-89096F62D36BQ36567202-9BE55F0F-3941-4FB7-B023-84302DEECD77Q42414532-385D4CDC-C497-4C29-A1B8-3C0D24135925Q45353637-1F9ACCBF-859D-4B2B-B3E7-0EF2C3695EF7Q47100073-533206CF-C87A-4BCD-B481-A31F5BC5B7FFQ48369065-E7E59233-1C99-423C-94F5-584540DD2B1BQ52613583-EB7ACE8A-6536-478D-A4DB-0B23391840A8
P2860
Studying the role of protein dynamics in an SN2 enzyme reaction using free-energy surfaces and solvent coordinates.
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Studying the role of protein d ...... faces and solvent coordinates.
@ast
Studying the role of protein d ...... faces and solvent coordinates.
@en
type
label
Studying the role of protein d ...... faces and solvent coordinates.
@ast
Studying the role of protein d ...... faces and solvent coordinates.
@en
prefLabel
Studying the role of protein d ...... faces and solvent coordinates.
@ast
Studying the role of protein d ...... faces and solvent coordinates.
@en
P2860
P50
P356
P1433
P1476
Studying the role of protein d ...... faces and solvent coordinates.
@en
P2093
J Javier Ruiz-Pernía
P2860
P2888
P304
P356
10.1038/NCHEM.1660
P577
2013-05-26T00:00:00Z
P6179
1001678147