Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
about
Divalent cations and the electrostatic potential around DNA: Monte Carlo and Poisson-Boltzmann calculations.Advantage of being a dimer for Serratia marcescens endonucleaseProtein charge and mass contribute to the spatio-temporal dynamics of protein-protein interactions in a minimal proteome.Assigning the protonation states of the key aspartates in β-Secretase using QM/MM X-ray structure refinementFruitful and futile encounters along the association reaction between proteins
P2860
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
description
1997 nî lūn-bûn
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1997年の論文
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年學術文章
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name
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@en
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@nl
type
label
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@en
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@nl
prefLabel
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@en
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@nl
P2093
P2860
P1433
P1476
Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease.
@en
P2093
Antosiewicz J
McCammon JA
P2860
P304
P356
10.1002/(SICI)1097-0282(19970405)41:4<443::AID-BIP8>3.0.CO;2-M
P577
1997-04-01T00:00:00Z