Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
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A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure.Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased SequencesA Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar StructurePropensities of peptides containing the Asn-Gly segment to form β-turn and β-hairpin structuresPropensities to form the β-turn and β-hairpin structures ofd-Pro-Gly and Aib-d-Ala containing peptides: a computational studyNature of aryl–tyrosine interactions contribute to β-hairpin scaffold stability: NMR evidence for alternate ring geometryAsymmetric Contribution of Aromatic Interactions Stems from Spatial Positioning of the Interacting Aryl Pairs in β-HairpinsComparative analysis of cross strand aromatic–Phe interactions in designed peptide β-hairpins
P2860
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P2860
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
description
2013 nî lūn-bûn
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name
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@en
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@nl
type
label
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@en
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@nl
prefLabel
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@en
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@nl
P2093
P2860
P356
P1476
Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.
@en
P2093
Narayanaswamy Shamala
Padmanabhan Balaram
Subrayashastry Aravinda
Upadhyayula S Raghavender
Veldore V Harini
P2860
P304
P356
10.1039/C3OB25777K
P577
2013-07-01T00:00:00Z