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Toniolo C.
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http://hub.abes.fr/acs/periodical/mamobx/1991/volume_24/issue_14/101021ma00014a006/authorship/1
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http://hub.abes.fr/acs/periodical/jacsat/1982/volume_104/issue_9/101021ja00373a018/authorship/8
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http://hub.abes.fr/acs/periodical/mamobx/1993/volume_26/issue_8/101021ma00060a028/authorship/7
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http://hub.abes.fr/springer/periodical/11224/1991/volume_2/issue_5/B937B7D09EDD5EAFE053120B220A9FCB/authorship/8
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http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_26/101021bi00240a026/authorship/3
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Author
of
Structural versatility of peptides from C.alpha.,.alpha.-dialkylated glycines. A conformational energy computation and x-ray diffraction study of homopeptides from 1-aminocyclohexane-1-carboxylic acid1
Conformational analysis of linear peptides. 2. A vapor-pressure osmometry study of self-association in chloroform
Stereochemically constrained peptides. Theoretical and experimental studies on the conformations of peptides containing 1-aminocyclohexanecarboxylic acid
Structural versatility of peptides from C.alpha.,.alpha.-dialkylated glycines. An infrared absorption and 1H nuclear magnetic resonance study of homopeptides from 1-aminocyclohexane-1-carboxylic acid1
Conformational analysis of linear peptides. 3. Temperature dependence of NH chemical shifts in chloroform
Chiroptical probes for configurational analysis of α-amino acids
Effects of Helical Distortions on the Optical Properties of Amide NH Infrared Absorption inShort Peptides in Solution
Agonist Activity at the Kinin B1 Receptor: Structural Requirements of theCentral Tetrapeptide
The Bip Method, Based on the Induced Circular Dichroism of a Flexible Biphenyl Probe in Terminally Protected -Bip-Xaa*- Dipeptides, for Assignment of the Absolute Configuration of β-Amino Acids
X-ray Diffraction Analysis and Conformational Energy Computations ofβ-Turn and 310-Helical Peptides Based on α-Amino Acids with anOlefinic Side Chain. Implications for Ring-Closing Metathesis
Self-Assembling Properties of Membrane-Modifying Peptides Studiedby PELDOR and CW-ESR Spectroscopies
Two-Dimensional Infrared Spectral Signatures of 310- and α-Helical Peptides
Preferred structures of constrained peptides from achiral α,α-dialkyiated glycyl residues with acyclic side chains
Turn and Helical Peptide Handedness Governed Exclusively by Side-ChainChiral Centers
Gold Nanoclusters Protected by ConformationallyConstrained Peptides
Induced Axial Chirality in the Biphenyl Core of theCα-Tetrasubstituted α-Amino Acid Residue Bip andSubsequent Propagation of Chirality in (Bip)n/ValOligopeptides
Role of Secondary Structure in the Asymmetric AcylationReaction Catalyzed by Peptides Based on ChiralCα-Tetrasubstituted α-Amino Acids
Facile and E-Selective Intramolecular Ring-Closing Metathesis Reactions in310-Helical Peptides: A 3D Structural Study
Crystal-state conformation of homo-oligomers of α-aminoisobutyric acid: Molecular and crystal structure of pBrBz-(Aib)6-OMe
First unequivocal observation of the multiple fully extended conformation (25-helix) in a homopeptide from a Cα-methylated chiral α-amino acid
Studies of peptides forming 310- and .alpha.-helixes and .beta.-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy
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