Extraordinarily robust polyproline type I peptoid helices generated via the incorporation of α-chiral aromatic N-1-naphthylethyl side chains.
about
Adding diverse noncanonical backbones to rosetta: enabling peptidomimetic designTriangular prism-shaped β-peptoid helices as unique biomimetic scaffoldsPrecisely tuneable energy transfer system using peptoid helix-based molecular scaffold.A rotamer library to enable modeling and design of peptoid foldamers.Synthesis and screening of stereochemically diverse combinatorial libraries of peptide tertiary amides.Split-and-pool synthesis and characterization of peptide tertiary amide libraryDe novo structure prediction and experimental characterization of folded peptoid oligomers.A peptoid ribbon secondary structure.Peptide and peptoid foldamers in medicinal chemistry.Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids.The n → π* interaction: a rapidly emerging non-covalent interaction.A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor rpn13 is toxic to multiple myeloma cellsAn overview of peptide and peptoid foldamers in medicinal chemistry.Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides.PPII Helical Peptidomimetics Templated by Cation-π Interactions.Macrocyclic peptoid-Peptide hybrids as inhibitors of class I histone deacetylases.Reciprocal carbonyl-carbonyl interactions in small molecules and proteins.Gadolinium-binding cyclic hexapeptoids: synthesis and relaxometric properties.Control of porphyrin interactions via structural changes of a peptoid scaffold.One-Bead-Two-Compound Thioether Bridged Macrocyclic γ-AApeptide Screening Library against EphA2.A Pure Polyproline Type I-like Peptoid Helix by Metal Coordination.Chemoselective fragment condensation between peptide and peptidomimetic oligomers.Construction and conformational behavior of peptoids with cis-amide bond geometry: design of a peptoid with alternate φ, ψ values of inverse PP-II/PP-II and PP-I structures.Osmoprotective polymer additives attenuate the membrane pore-forming activity of antimicrobial peptoids.Peptoid helicity modulation: precise control of peptoid secondary structures via position-specific placement of chiral monomers.Design of Peptoid-peptide Macrocycles to Inhibit the β-catenin TCF Interaction in Prostate CancerHomooligomers of substituted prolines and β-prolines: syntheses and secondary structure investigation
P2860
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P2860
Extraordinarily robust polyproline type I peptoid helices generated via the incorporation of α-chiral aromatic N-1-naphthylethyl side chains.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
Extraordinarily robust polypro ...... N-1-naphthylethyl side chains.
@en
type
label
Extraordinarily robust polypro ...... N-1-naphthylethyl side chains.
@en
prefLabel
Extraordinarily robust polypro ...... N-1-naphthylethyl side chains.
@en
P2093
P2860
P356
P1476
Extraordinarily robust polypro ...... N-1-naphthylethyl side chains.
@en
P2093
Helen E Blackwell
Ilia A Guzei
J Aaron Crapster
Joseph R Stringer
P2860
P304
15559-15567
P356
10.1021/JA204755P
P407
P577
2011-09-13T00:00:00Z