Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

about

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

Item

http://www.wikidata.org/entity/Q48543667

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@en

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@nl

type

Item

label

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@en

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@nl

prefLabel

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@en

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@nl

P1476

Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.

@en

P2093

Claudia Di Salvo

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

Donatella Diana

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

Lucia De Rosa

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

Roberto Fattorusso

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

Veronica Celentano

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

P2860

Tryptophan zippers: Stable, monomeric -hairpins

A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

A short linear peptide that folds into a native stable beta-hairpin in aqueous solution

The geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.

Aromatic interactions in peptides: impact on structure and function.

The design, structures and therapeutic potential of protein epitope mimetics.

Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.

Selective aromatic interactions in beta-hairpin peptides.

AutoLink: automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic.

P304

787-795

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

P31

scholarly article

P356

10.1039/C7OB02815F

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

P433

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

P478

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

P50

Alessandra Romanelli

Luca D D'Andrea

P577

2018-01-10T00:00:00Z

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

P698

29319097

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