Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

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Biological consequences of improving the structural stability of hairpins that have antimicrobial activity.

P2860

Q48201156-449B4D31-DC5D-404B-9ED1-80B997373B43

P2860

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

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http://www.wikidata.org/entity/Q47130278

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2016 nî lūn-bûn

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2016年の論文

@ja

2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

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Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@en

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

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Item

label

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@en

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@nl

prefLabel

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@en

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@nl

P1476

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

@en

P2093

Brandon L Kier

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

Kalkena Sivanesam

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

Niels H Andersen

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

Samuel D Whedon

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

P2860

The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider

Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

An improved capping unit for stabilizing the ends of associated β-strands.

Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin.

Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding

Stabilizing capping motif for beta-hairpins and sheets.

Induction of cancer cell death by self-assembling nanostructures incorporating a cytotoxic peptide.

Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure.

Mechanisms of antimicrobial peptide action and resistance.

P304

4480-4488

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P31

scholarly article

P356

10.1002/1873-3468.12477

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

P407

English

P433

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

P478

590

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

P50

Champak Chatterjee

P577

2016-11-09T00:00:00Z

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P698

27859052

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P932

5578868

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Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

about

P2860

P2860

Hairpin structure stability plays a role in the activity of two antimicrobial peptides.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932