The role of electrostatic interaction in triggering the unraveling of stable helix 1 in normal prion protein. A molecular dynamics simulation investigation.
about
Highly polar environments catalyze the unfolding of PrP C helix 1.Copper binding sites in the C-terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study.The effect of heme on the conformational stability of micro-myoglobin.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.
P2860
The role of electrostatic interaction in triggering the unraveling of stable helix 1 in normal prion protein. A molecular dynamics simulation investigation.
description
2005 nî lūn-bûn
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2005年の論文
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name
The role of electrostatic inte ...... mics simulation investigation.
@en
The role of electrostatic inte ...... mics simulation investigation.
@nl
type
label
The role of electrostatic inte ...... mics simulation investigation.
@en
The role of electrostatic inte ...... mics simulation investigation.
@nl
prefLabel
The role of electrostatic inte ...... mics simulation investigation.
@en
The role of electrostatic inte ...... mics simulation investigation.
@nl
P2093
P2860
P1476
The role of electrostatic inte ...... mics simulation investigation.
@en
P2093
Hong-Fang Ji
Hong-Yu Zhang
Liang Shen
P2860
P304
P356
10.1080/07391102.2005.10507026
P577
2005-04-01T00:00:00Z