Propensities of peptides containing the Asn-Gly segment to form β-turn and β-hairpin structures

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On the intrinsic propensity of the Asn-Gly sequence to fold into type I' β-turn: molecular dynamics simulations of Asn-Gly β-turn containing peptide sequences.Propensities to form the β-turn and β-hairpin structures ofd-Pro-Gly and Aib-d-Ala containing peptides: a computational study

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Q50020035-12CCBC64-CFD6-4226-9044-0874E58700D6 Q57697343-E8369189-DE57-49C3-AC63-5E5DB3EB1414

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Propensities of peptides containing the Asn-Gly segment to form β-turn and β-hairpin structures

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http://www.wikidata.org/entity/Q57697339

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scientific article published on 01 September 2016

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wetenschappelijk artikel

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наукова стаття, опублікована в червні 2016

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name

Propensities of peptides conta ...... -turn and β-hairpin structures

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Propensities of peptides conta ...... -turn and β-hairpin structures

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type

Item

label

Propensities of peptides conta ...... -turn and β-hairpin structures

@en

Propensities of peptides conta ...... -turn and β-hairpin structures

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Propensities of peptides conta ...... -turn and β-hairpin structures

@en

Propensities of peptides conta ...... -turn and β-hairpin structures

@nl

P1476

Propensities of peptides conta ...... -turn and β-hairpin structures

@en

P2093

In Kee Yoo

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

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Tryptophan zippers: Stable, monomeric -hairpins

Influence of local interactions on protein structure. I. Conformational energy studies of N-acetyl-N'-methylamides of Pro-X and X-Pro dipeptides.

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.

Nonstereogenic alpha-aminoisobutyryl-glycyl dipeptidyl unit nucleates type I' beta-turn in linear peptides in aqueous solution.

Beta-hairpin peptidomimetics: design, structures and biological activities.

Solvent-induced beta-hairpin to helix conformational transition in a designed peptide.

Chirality-controlled formation of beta-turn secondary structures in short peptide chains: gas-phase experiment versus quantum chemistry.

Conformational preference and cis-trans isomerization of 4-methylproline residues.

Conformational preferences of X-Pro sequences: Ala-Pro and Aib-Pro motifs.

Beta-hairpin families in globular proteins.

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653-664

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scholarly article

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10.1002/BIP.22863

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

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105

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

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Young Kee Kang

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2016-09-01T00:00:00Z

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27122246

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Biofiseg

Propensities of peptides containing the Asn-Gly segment to form β-turn and β-hairpin structures

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P2860

P2860

Propensities of peptides containing the Asn-Gly segment to form β-turn and β-hairpin structures

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921