Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding

Keyphrases

• SH2 Domain 100%
• Peptide Inhibitor 100%
• Propylene 100%
• Conformationally Constrained Peptides 100%
• Trisubstituted 100%
• Peptide Mimics 80%
• Conformationally Constrained 40%
• SH3 Domain 20%
• X-ray Crystallography 20%
• K(I) 20%
• Thermodynamics 20%
• Src Kinase 20%
• Bound States 20%
• Binding Parameters 20%
• Derived Peptide 20%
• Isothermal Titration Calorimetry 20%
• Phosphotyrosine 20%
• Binding Thermodynamics 20%
• Tetrapeptide 20%
• Binding Interface 20%
• Conformational Variation 20%
• Rigorous Analysis 20%
• Thermodynamic Data 20%
• Peptide Binding Modes 20%
• Buried Surface Area 20%
• Cyclopropane Ring 20%
• Flexible Ligand 20%
• Isostere 20%

Biochemistry, Genetics and Molecular Biology

• Binding Domain 100%
• SH2 Domain 100%
• Cyclopropane 100%
• Surface Area 50%
• Enthalpy 50%
• Crystal Structure 25%
• Kinase 25%
• Phosphotransferase 25%
• Energy Transfer 25%
• X-Ray Crystallography 25%
• Isothermal Titration Calorimetry 25%
• Tetrapeptide 25%