Monitoring protein conformational changes by quenching of intrinsic fluorescence.
The quenching of intrinsic fluorescence of human serum albumin and pigeon liver malic enzyme by acrylamide was studied after the proteins were denatured to different stages. The progress of protein denaturation induced by guanidine hydrochloride was accompanied by increasing of effective dynamic quenching constant which provides a convenient parameter for monitoring protein conformational change.
D020106:Acrylamide; D000178:Acrylamides; D000818:Animals; D010856:Columbidae; D006801:Humans; D008099:Liver / Q000201:enzymology; D008291:Malate Dehydrogenase; D011487:Protein Conformation; D011489:Protein Denaturation; D012709:Serum Albumin; D013050:Spectrometry, Fluorescence / Q000379:methods*
D000178:Acrylamides; D012709:Serum Albumin; D020106:Acrylamide; D008291:Malate Dehydrogenase