Protein fluorescence decay: a gamma function description of thermally induced interconversion of amino acid rotamers.
We present a description of fluorescence decay kinetics in complex environments based on gamma functions rather than the conventional approach using exponentials. The gamma function description is tested in measurements on the temperature dependence of the protein human serum albumin (HSA), N-acetyl tryptophanamide (NATA), and 2, 5-dipenyl oxazole (PPO). The monitoring of macromolecular structure and dynamics is demonstrated by means of distinct tryptophan (Trp) rotamer populations and their interconversion in HSA.
Rolinski
Olaf J
OJ
Department of Physics, Scottish Universities Physics Alliance, Photophysics Group, University of Strathclyde, John Anderson Building, 107 Rottenrow, Glasgow G4 0NG, United Kingdom.
Scobie
Katherine
K
Birch
David J S
DJ
D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000648:ultrastructure*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry*
D000596:Amino Acids; D012709:Serum Albumin; D014364:Tryptophan