Folding of peptides characterized by c3Val, a highly constrained analogue of valine(465 views) Peggion C, Formaggio F, Crisma M, Toniolo C, Jimenez AI, Cativiela C, Kaptein B, Broxterman QB, Saviano M, Benedetti E
Keywords: β-Bend, 310-Helix, Amino Acid Synthesis, Cα-Tetrasubstituted α-Amino Acids, Conformational Analysis, Cyclopropane Amino Acid, Ir Absorption, Peptide Synthesis, X-Ray Diffraction, Fourier Transform Infrared Spectroscopy, Synthesis (chemical), X Ray Diffraction, Chirality, Amino Acid Derivative, Glycine, Valine, Article, Biosynthesis, Crystal Structure, Enantiomer, Intermethod Comparison, Methylation, Protein Analysis, Protein Folding, Protein Structure, Crystallography, Models, Molecular, Molecular Conformation, Oligopeptides, Protein Conformation, ß-Bend, Ca-Tetrasubstituted A-Amino Acids,
Affiliations: *** IBB - CNR ***
Institute of Biomolecular Chemistry, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy
DSM Fine Chemicals, Advanced Synthesis and Catalysis, P. O. Box 18, 6160 MD Geleen, Netherlands
Inst. of Biostructures/Bioimaging, Department of Chemistry, University of Naples Federico II, 80134 Naples, Italy
References: Not available.
Folding of peptides characterized by c3Val, a highly constrained analogue of valine