Changes in Calorimetric Parameters and Solvent Accessibility of Hydrophobic Groups in Native and Chemically Modified Immunoglobulin G

Keyphrases

• Immunoglobulin G 100%
• Chemically Modified 100%
• Dynamic Light Scattering 100%
• Solvent Accessibility 100%
• Hydrophobic Group 100%
• Alkyl Group 50%
• Covalent Modification 50%
• Intramolecular Interactions 50%
• Aqueous Solution 50%
• Molecular Structure 50%
• Protein-protein Interaction 50%
• Scattered Data 50%
• Esters 50%
• Aggregate Size 50%
• Differential Scanning Calorimetry 50%
• Structural Rearrangement 50%
• N-hydroxysuccinimide 50%
• Hydrophobicity Index 50%
• Surface Hydrophobicity 50%
• Spontaneous Aggregation 50%
• Alkyl Chain 50%
• Modification Degree 50%
• Human IgG 50%
• Tmax 50%
• Maximal Deviation 50%
• Heat Flow 50%
• Caprylic 50%
• Spectrofluorimetry 50%
• Thermogram 50%
• ANS Binding 50%

Material Science

• Rigidity 100%
• Solution 100%
• Differential Scanning Calorimetry 100%
• Fluorescence Spectroscopy 100%
• Hydrophobicity 100%
• Covalent Modification 100%
• Molecular Structure 100%
• Surface (Surface Science) 100%

Chemistry

• Photon Correlation Spectroscopy 100%
• Alkyl Group 50%
• Molecular Structure 50%
• Fluorescence Spectroscopy 50%
• Hydrophobicity 50%
• Protein Interaction 50%
• Differential Scanning Calorimetry 50%
• Tmax 50%
• Aqueous Solution 50%
• Solution 50%