Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: Computational analysis and protein engineering

Keyphrases

• Computational Analysis 100%
• Protein Engineering 100%
• Heat Shock Protein 70 (HSP70) 100%
• Electrostatic Interaction 100%
• Heat Shock Protein 90 (Hsp90) 100%
• Tetratricopeptide 100%
• Free Energy Perturbation 75%
• Electrostatic Calculations 50%
• Perturbation Calculation 50%
• TPR Domain 50%
• Anticancer Drugs 25%
• Molecular Dynamics Simulation 25%
• Site-directed mutagenesis 25%
• Binding Affinity 25%
• Hsp70 Chaperone 25%
• Ligand Binding 25%
• C-terminus 25%
• Binding Pocket 25%
• Result Accuracy 25%
• Substrate Proteins 25%
• Charged Residue 25%
• Protein Design 25%
• Unfavorable Interaction 25%
• Noncognate 25%
• Peptide Recognition 25%
• Domain Peptide 25%
• Continuum Electrostatics 25%
• Poisson-Boltzmann Electrostatics 25%
• Buried Residues 25%
• Fold Increase 25%
• Oncogenic Proteins 25%
• Chaperone Hsp90 25%
• Peptide Interaction 25%
• Significant Target 25%
• TPR1 25%

Biochemistry, Genetics and Molecular Biology

• Hsp90 100%
• Hsp70 100%
• Static Electricity 100%
• Tetratricopeptide 100%
• Protein Engineering 100%
• Ligand Binding 40%
• TPR Domain 40%
• Dynamics 20%
• Crystal Structure 20%
• Protein Domain 20%
• Protein Design 20%
• Maturation 20%
• C-Terminus 20%
• Binding Affinity 20%
• Site-Directed Mutagenesis 20%