Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions.
about
Nanopore analysis of wild-type and mutant prion protein (PrP(C)): single molecule discrimination and PrP(C) kinetics.Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.Mapping the early steps in the pH-induced conformational conversion of the prion protein.Prion and water: tight and dynamical hydration sites have a key role in structural stability.Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases.Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: insight into dynamics and propertiesInfluence of pH on the human prion protein: insights into the early steps of misfolding.Effect of atom- and group-based truncations on biomolecules simulated with reaction-field electrostatics.Toward the correction of effective electrostatic forces in explicit-solvent molecular dynamics simulations: restraints on solvent-generated electrostatic potential and solvent polarization.PrP charge structure encodes interdomain interactionsInsight into Early-Stage Unfolding of GPI-Anchored Human Prion Protein.The consequences of pathogenic mutations to the human prion protein.Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysisDifferential stability of the bovine prion protein upon urea unfoldingClassical electrostatics for biomolecular simulations.In silico strategies on prion pathogenic conversion and inhibition from PrPC -PrPSc.On the truncation of long-range electrostatic interactions in DNA.Computational studies on prion proteins: effect of Ala(117)-->Val mutation.Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: effect of protonation of histidine residues.Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study.Monitoring prion protein stability by NMR.The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein.The role of electrostatic interaction in triggering the unraveling of stable helix 1 in normal prion protein. A molecular dynamics simulation investigation.Investigation of the effect of glycosylation on human prion protein by molecular dynamics.On the Ewald artifacts in computer simulations. The test-case of the octaalanine peptide with charged termini.Sequence-dependent dynamical instability of the human prion protein: a comparative simulation study.Electrostatics in the stability and misfolding of the prion protein: salt bridges, self energy, and solvation.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.β-sheet-like formation during the mechanical unfolding of prion protein.
P2860
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P2860
Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Molecular dynamics simulations ...... of electrostatic interactions.
@ast
Molecular dynamics simulations ...... of electrostatic interactions.
@en
type
label
Molecular dynamics simulations ...... of electrostatic interactions.
@ast
Molecular dynamics simulations ...... of electrostatic interactions.
@en
prefLabel
Molecular dynamics simulations ...... of electrostatic interactions.
@ast
Molecular dynamics simulations ...... of electrostatic interactions.
@en
P356
P1433
P1476
Molecular dynamics simulations ...... of electrostatic interactions.
@en
P2093
P304
13862-13876
P356
10.1021/BI991469D
P407
P577
1999-10-01T00:00:00Z