Keywords: Cyclic Peptides, Nmr, Protein Tyrosine Phosphatase, Yersinia, Yersinia Outer Protein H, Aspartic Acid, Cyclopeptide, Lysine, Phosphotyrosine, Protein Yop H, Unclassified Drug, Amino Terminal Sequence, Binding Affinity, Controlled Study, Cyclization, Drug Design, Nonhuman, Nuclear Magnetic Resonance, Priority Journal, Protein Motif, Protein Protein Interaction, Yersinia Infection, Bacterial Outer Membrane Proteins, Escherichia Coli, Kinetics, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Binding, Protein Interaction Domains And Motifs, Recombinant Fusion Proteins,
Affiliations: *** IBB - CNR ***
Infectious and Inflammatory Disease Center and Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, 92037 La Jolla, CA, United States
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
References: Not available.
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH