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Proceedings Paper

Time- and temperature-dependent fluorescence anisotropy study of a single-tyrosne protein and a model compound
Author(s): Xiao-Yuan Liu; Thomas M. Nordlund
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Paper 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.

Paper Details

Date Published: 1 May 1990
PDF: 7 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17777
Show Author Affiliations
Xiao-Yuan Liu, Univ. of Rochester (United States)
Thomas M. Nordlund, Univ. of Rochester (United States)

Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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