Investigation of conformational changes in proteins using fluorescence and fluorescence anisotropy decay

摘要

Several well-characterized conformational changes in two proteins, bovine serum albumin and yeast enolase. were investigated using steady-state quenching and dynamic fluorescence measurements. These results were compared with published observations. Conformational changes involving domain or subunit separation are associated with increased Stern-Volmer quenching constants but no consistent change in emission maximum or average tryptophanyl-fluorescence lifetime. Rotational correlation times from tryptophanyl-fluorescence anisotropy decay are in agreement with expected values, showing the value of such measurements in analysis of conformational changes in proteins.