Sequential and competitive adsorption of peptides at pendant PEO layers.

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Sequential and competitive adsorption of peptides at pendant PEO layers.

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2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

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name

Sequential and competitive adsorption of peptides at pendant PEO layers.

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Sequential and competitive adsorption of peptides at pendant PEO layers.

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label

Sequential and competitive adsorption of peptides at pendant PEO layers.

@ast

Sequential and competitive adsorption of peptides at pendant PEO layers.

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Sequential and competitive adsorption of peptides at pendant PEO layers.

@ast

Sequential and competitive adsorption of peptides at pendant PEO layers.

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P1476

Sequential and competitive adsorption of peptides at pendant PEO layers

@en

P2093

Joseph McGuire

http://www.w3.org/2001/XMLSchema#string

Joshua L Snider

http://www.w3.org/2001/XMLSchema#string

Matthew P Ryder

http://www.w3.org/2001/XMLSchema#string

Xiangming Wu

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P2860

Polyproline-II helix in proteins: structure and function.

Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect.

Effect of secondary structure on the potential of mean force for poly-L-lysine in the alpha-helix and beta-sheet conformations.

Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.

Evaluation of WLBU2 peptide and 3-O-octyl-sn-glycerol lipid as active ingredients for a topical microbicide formulation targeting Chlamydia trachomatis.

Concentration effects on peptide elution from pendant PEO layers

Activity of the de novo engineered antimicrobial peptide WLBU2 against Pseudomonas aeruginosa in human serum and whole blood: implications for systemic applications.

History dependence of protein adsorption kinetics.

Probing the orientation of surface-immobilized protein G B1 using ToF-SIMS, sum frequency generation, and NEXAFS spectroscopy.

The helical hydrophobic moment: a measure of the amphiphilicity of a helix.

P304

69-76

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.COLSURFB.2015.04.011

http://www.w3.org/2001/XMLSchema#string

P478

130

http://www.w3.org/2001/XMLSchema#string

P50

Karl F Schilke

P577

2015-04-14T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

25909181

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P932

4457692

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