Hydrophobic Affinity Partitioning as a Method for Studying Conformational Changes in Proteins
Hydrophobic interactions are important for the stability, conformation and function of proteins. The biological function of many proteins, including enzymes and the stability of multimeric proteins and protein complexes is regulated by a change in conformation and a concommitant change in surface hydrophobicity induced by the binding of ions or ligands.
KeywordsFatty Ester Hydrophobic Site Hydrophobic Ligand Protein Surface Hydrophobicity Partition Curve
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