Structural characteristics of alpha-helical peptide molecules containing Aib residues.
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Models for the 3(10)-helix/coil, pi-helix/coil, and alpha-helix/3(10)-helix/coil transitions in isolated peptidesNMR structure of the channel-former zervamicin IIB in isotropic solventsThe NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micellesSpatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gatingShort constrained peptides that inhibit HIV-1 entryHelix-stabilized cyclic peptides as selective inhibitors of steroid receptor-coactivator interactionsThe Trp-cage: optimizing the stability of a globular miniproteinThe crystal structure of samarosporin I at atomic resolutionInsight into the Structural and Biological Relevance of the T/R Transition of the N-Terminus of the B-Chain in Human InsulinStructure-activity relation of NH2-terminal human parathyroid hormone fragmentsConformational restriction through C alpha i C alpha i cyclization: Ac12c, the largest cycloaliphatic C alpha,alpha- disubstituted glycine knownFrozen, but no accident - why the 20 standard amino acids were selected.De novo design, synthesis and solution conformational study of two didehydroundecapeptides: effect of nature and number of amino acids interspersed between ΔPhe residues.Energy transport in peptide helicesSpectroscopically labeled peptaibiotic analogs: the 4-nitrophenylalanine infrared absorption probe inserted at different positions into trichogin GA IV.Context-dependent conformation of diethylglycine residues in peptides.A method for computational combinatorial peptide design of inhibitors of Ras protein.Water-solubilized, cap-stabilized, helical polyalanines: calibration standards for NMR and CD analyses.Interaction between TOAC free radical and photoexcited triplet chromophores linked to peptide templates.Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides.Preferred conformation of peptides based on cycloaliphatic C(alpha,alpha)-disubstituted glycines: 1-amino-cycloundecane-1-carboxylic acid (Ac11c).Solvent-induced beta-hairpin to helix conformational transition in a designed peptide.Crystal structure of a hydrophobic 19-residue peptide helix containing three centrally located D amino acids.De novo design: backbone conformational constraints in nucleating helices and beta-hairpins.Parallel zippers formed by alpha-helical peptide columns in crystals of Boc-Aib-Glu(OBzl)-Leu-Aib-Ala-Leu-Aib-Ala-Lys(Z)-Aib-OMe.3(10) helices in channels and other membrane proteinsExploration of the structural features defining the conduction properties of a synthetic ion channel.The role of alpha-, 3(10)-, and pi-helix in helix-->coil transitions.Control of peptide conformation by the Thorpe-Ingold effect (C alpha-tetrasubstitution).De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold.(α,α-dimethyl)glycyl (dmg) PNAs: achiral PNA analogs that form stronger hybrids with cDNA relative to isosequential RNA.Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment.Diffusion NMR spectroscopy: folding and aggregation of domains in p53.Facile transition between 3(10)- and alpha-helix: structures of 8-, 9-, and 10-residue peptides containing the -(Leu-Aib-Ala)2-Phe-Aib- fragment.Impact of the amino acid sequence on the conformation of side chain lactam-bridged octapeptides.Inhibition of caspase-9 by stabilized peptides targeting the dimerization interface.Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of alpha-amino acidsEfforts toward deriving the CD spectrum of a 3(10) helix in aqueous medium.
P2860
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P2860
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
description
article científic
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article scientifique
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articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@en
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@nl
type
label
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@en
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@nl
prefLabel
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@en
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@nl
P356
P1433
P1476
Structural characteristics of alpha-helical peptide molecules containing Aib residues.
@en
P2093
P304
P356
10.1021/BI00481A001
P407
P577
1990-07-01T00:00:00Z