Fold-unfold transitions in the selectivity and mechanism of action of the N-terminal fragment of the bactericidal/permeability-increasing protein (rBPI(21)).
about
rBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes.The pH sensitivity of histidine-containing lytic peptidesDistribution, transition and thermodynamic stability of protein conformations in the denaturant-induced unfolding of proteins.Potential strategies for the eradication of multidrug-resistant Gram-negative bacterial infections.
P2860
Fold-unfold transitions in the selectivity and mechanism of action of the N-terminal fragment of the bactericidal/permeability-increasing protein (rBPI(21)).
description
2009 nî lūn-bûn
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2009年の論文
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2009年論文
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2009年論文
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name
Fold-unfold transitions in the ...... increasing protein (rBPI(21)).
@en
Fold-unfold transitions in the ...... ermeability-increasing protein
@nl
type
label
Fold-unfold transitions in the ...... increasing protein (rBPI(21)).
@en
Fold-unfold transitions in the ...... ermeability-increasing protein
@nl
prefLabel
Fold-unfold transitions in the ...... increasing protein (rBPI(21)).
@en
Fold-unfold transitions in the ...... ermeability-increasing protein
@nl
P2860
P50
P1433
P1476
Fold-unfold transitions in the ...... increasing protein (rBPI(21)).
@en
P2093
Miguel A R B Castanho
Sílvia C D N Lopes
P2860
P304
P356
10.1016/J.BPJ.2008.10.044
P407
P577
2009-02-01T00:00:00Z