De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.
about
Total sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleasesMapping the Geometric Evolution of Protein Folding MotorCrystal structure of a hydrophobic 19-residue peptide helix containing three centrally located D amino acids.Infinite pleated beta -sheet formed by the beta-hairpin Boc-beta-Phe-beta-Phe-D-Pro-Gly-beta-Phe-beta-Phe-OMe.Peptide hairpins with strand segments containing alpha- and beta-amino acid residues: cross-strand aromatic interactions of facing Phe residues.De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: Compaction mediated by weak interactionsPeptide hybrids containing alpha - and beta-amino acids: structure of a decapeptide beta-hairpin with two facing beta-phenylalanine residuesDesign of symmetric TIM barrel proteins from first principles.A second look at mini-protein stability: analysis of FSD-1 using circular dichroism, differential scanning calorimetry, and simulations.Quantum kernel applications in medicinal chemistry.Analysis of residue conformations in peptides in Cambridge structural database and protein-peptide structural complexes.Molecular carpentry: piecing together helices and hairpins in designed peptides.Effects of hydrogen-bond deletion on peptide helices: structural characterization of depsipeptides containing lactic acid.Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.Propensities 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
De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.
description
2000 nî lūn-bûn
@nan
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
De novo protein design: crysta ...... t helical and hairpin domains.
@ast
De novo protein design: crysta ...... t helical and hairpin domains.
@en
type
label
De novo protein design: crysta ...... t helical and hairpin domains.
@ast
De novo protein design: crysta ...... t helical and hairpin domains.
@en
prefLabel
De novo protein design: crysta ...... t helical and hairpin domains.
@ast
De novo protein design: crysta ...... t helical and hairpin domains.
@en
P2093
P2860
P356
P1476
De novo protein design: crysta ...... t helical and hairpin domains.
@en
P2093
P2860
P304
P356
10.1073/PNAS.97.7.3034
P407
P577
2000-03-01T00:00:00Z