Contents
Noncovalent Forces Important to the Conformational Stability of Protein Structures.
Degradative Covalent Reactions Important to Protein Stability Fluorescence Spectroscopy.
Ultraviolet Absorption Spectroscopy.
Circular Dichroism.
Infrared Spectroscopy.
Identifying Sites of Posttranslational Modifications in Proteins via HPLC Peptide Mapping.
Urea and Guanidine Hydrochloride Denaturation Curves.
Differential Scanning Calorimetry.
Disulfide Bonds in Protein Folding and Stability.
Solvent Stabilization of Protein Structure.
Site-Directed Mutagenesis to Study Protein Folding and Stability.
Hydrogen Exchange Techniques.
Protein Folding Kinetics.
Molten Globules.
Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES.