Microcalorimetric studies of the mechanism of interaction between designed peptides and hydrophobic adsorbents

Keyphrases

• Interaction Mechanism 100%
• Microcalorimetric 100%
• Octyl-Sepharose 100%
• Hydrophobic Adsorbent 100%
• Designer Peptides 100%
• Adsorbent 75%
• Hydrophobic Ligand 75%
• Heat of Dilution 75%
• Adsorption 50%
• Tryptophan 50%
• Adsorption Mechanism 50%
• Entropy-driven 50%
• Binding Affinity 25%
• Thermodynamic Parameters 25%
• Chain Length 25%
• Amino Acid Residues 25%
• Adsorption Behavior 25%
• Peptide Purification 25%
• Equilibrium Binding 25%
• Binding Isotherm 25%
• Isotherm Analysis 25%
• Tryptophan Residues 25%
• Solvation 25%
• Binding Thermodynamics 25%
• Binding Analysis 25%
• Hydrophobic Interaction 25%
• Adsorption Enthalpy 25%
• Binding Enthalpy 25%
• Solvation Behaviour 25%
• Buffer System 25%
• Enthalpy-driven 25%
• Residue Behavior 25%
• Cation-anion Interaction 25%
• Peptide Drug Design 25%
• Batch Equilibrium 25%
• Buffer Effect 25%
• Heat Measurement 25%

Chemistry

• Adsorbent 100%
• Buffer Solution 75%
• Dilution 75%
• Tryptophan 75%
• Enthalpy 50%
• Solvation 50%
• Adsorption Behavior 25%
• Kd 25%
• Adsorption Enthalpy 25%
• Oligomer 25%
• Amino Acid 25%

Biochemistry, Genetics and Molecular Biology

• Enthalpy 100%
• Dilution 100%
• Tryptophan 100%
• Solution and Solubility 66%
• Solvation 66%
• Binding Affinity 33%
• Amino Acids 33%
• Copurification 33%