1 May 1990 Time- and temperature-dependent fluorescence anisotropy study of a single-tyrosne protein and a model compound
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Abstract
A possible ultrafast rotational motion of the phenol ring of buried tyrosine residue 69 in lima bean trypsin/chymotrypsin inhibitor (LBI) was observed in addition to a 40-ps restricted rotational motion and the overall nanosecond protein rotation. A picosecond laser-streak camera system was used for short time resolution and measurements of the fluorescence anisotropy, r, vs. temperature, time and glycerol concentration were done by simultaneously recording both polarized tyrosine emission components. A variable-width square well was used to describe the temperature-dependent amplitude of the ultrafast process.
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Xiao-Yuan Liu, Xiao-Yuan Liu, Thomas M. Nordlund, Thomas M. Nordlund, "Time- and temperature-dependent fluorescence anisotropy study of a single-tyrosne protein and a model compound", Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17777; https://doi.org/10.1117/12.17777
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