Expected and unexpected results from combined beta-hairpin design elements.

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Stabilizing capping motif for beta-hairpins and sheets.Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.

P2860

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Expected and unexpected results from combined beta-hairpin design elements.

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http://www.wikidata.org/entity/Q44978959

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2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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name

Expected and unexpected results from combined beta-hairpin design elements.

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Expected and unexpected results from combined beta-hairpin design elements.

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type

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Expected and unexpected results from combined beta-hairpin design elements.

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Expected and unexpected results from combined beta-hairpin design elements.

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prefLabel

Expected and unexpected results from combined beta-hairpin design elements.

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Expected and unexpected results from combined beta-hairpin design elements.

@nl

P1476

Expected and unexpected results from combined beta-hairpin design elements.

@en

P2093

Muthu Dhanasekaran

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

Om Prakash

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

Paul W Baures

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

Yu Xi Gong

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

P2860

Energy landscape of a peptide consisting of alpha-helix, 3(10)-helix, beta-turn, beta-hairpin, and other disordered conformations

Molecular recognition of macrocyclic peptidomimetic inhibitors by HIV-1 protease

Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

Tryptophan zippers: Stable, monomeric -hairpins

Length-dependent stability and strand length limits in antiparallel -sheet secondary structure

Stability of cyclic beta-hairpins: asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair

Turn stability in β-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns

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 role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitin

P304

2071-2082

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scholarly article

P356

10.1039/B315228F

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

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P478

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

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2004-06-24T00:00:00Z

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

P698

15254635

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

Expected and unexpected results from combined beta-hairpin design elements.

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P2860

P2860

Expected and unexpected results from combined beta-hairpin design elements.

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