Induced conformational states of amphipathic peptides in aqueous/lipid environments.
about
Investigation of the effects of surface chemistry and solution concentration on the conformation of adsorbed proteins using an improved circular dichroism methodIonic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone proteinPeptide-column interactions and their influence on back exchange rates in hydrogen/deuterium exchange-MS.Stabilization of an alpha-helical conformation in an isolated hexapeptide inhibitor of calmodulin.Successful identification of novel agents to control infectious diseases from screening mixture-based peptide combinatorial libraries in complex cell-based bioassays.Statistical analysis and molecular dynamics simulations of ambivalent α-helices.Peptide binding domains determined through chemical modification of the side-chain functional groups.Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic indexStructure-guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomersImproved peptide elution time prediction for reversed-phase liquid chromatography-MS by incorporating peptide sequence information.Rapid identification of compounds with enhanced antimicrobial activity by using conformationally defined combinatorial libraries.Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries.Lysine-enriched cecropin-mellitin antimicrobial peptides with enhanced selectivityRequirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and locationIntrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales.Observed peptide pI and retention time shifts as a result of post-translational modifications in multidimensional separations using narrow-range IPG-IEF.Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents.The interaction of bioactive peptides with an immobilized phosphatidylcholine monolayer.Molecular dynamics study of the folding of hydrophobin SC3 at a hydrophilic/hydrophobic interface.Secondary Structure Determination of Peptides and Proteins After Immobilization.A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides.Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion.The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins.Mixed-mode hydrophilic interaction/cation-exchange chromatography: separation of complex mixtures of peptides of varying charge and hydrophobicity.Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1mm to 9.4mm I.D.).Controlled alteration of the shape and conformational stability of alpha-helical cell-lytic peptides: effect on mode of action and cell specificity.Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH).Conformational analysis of neuropeptide Y-[18-36] analogs in hydrophobic environments.Retro analog concept: comparative study on physico-chemical and biological properties of selected antimicrobial peptides.Design of peptide standards with the same composition and minimal sequence variation to monitor performance/selectivity of reversed-phase matrices.Rational design of peptides with anti-HCV/HIV activities and enhanced specificity.Structural properties of carnation mottle virus p7 movement protein and its RNA-binding domain.The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes.Influence of the hydrophilic face on the folding ability and stability of alpha-helix bundles: relevance to the peptide catalytic activity.Counter-ion effect on antistaphylococcal activity and cytotoxicity of selected antimicrobial peptides.An analysis of the helix-to-strand transition between peptides with identical sequence.The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.
P2860
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P2860
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@ast
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@en
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@nl
type
label
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@ast
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@en
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@nl
prefLabel
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@ast
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@en
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@nl
P2093
P2860
P1433
P1476
Induced conformational states of amphipathic peptides in aqueous/lipid environments.
@en
P2093
E Pérez-Payá
J M Ostresh
R A Houghten
S E Blondelle
P2860
P304
P356
10.1016/S0006-3495(95)80194-3
P407
P577
1995-01-01T00:00:00Z