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Proceedings Paper

Applications of KINDK: following macromolecular processes with lifetimes
Author(s): Susan M. Green; Preston Hensley; Jay R. Knutson
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Paper Abstract

The folding of proteins into a (single?) compact globular structure is an important mystery in contemporary biochemistry. It has even been referred to as the "second half" of the genetic code (1), since folding often provides the ultimate limit to genetic engineering. A variety of spectroscopies have been applied over the years, and stopped-flow steady-state fluorescence has contributed its share of information. Time-resolved fluorescence, however, is a newcomer to this endeavor. Realizing that time-correlated single photon counting (TCSPC) can provide lifetime resolution with only a few thousand photons, Brand & coworkers began to examine HLADH lifetimes during denaturation nearly a decade ago (2). The arc-lamp based technology used then was adequate to resolve changes requiring many minutes, and the early inclusion of global analysis in the process then called "KINDK" (3) extended the accuracy available. It was clear then that the advent of high repetition rate sources such as the modelocked, cavity-dumped dye laser would lead to improved accuracy and faster collection times. The HLADH system was revisited as soon as such technology was inhand (4).

Paper Details

Date Published: 1 May 1990
PDF: 12 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17687
Show Author Affiliations
Susan M. Green, Georgetown Univ. (United States)
Preston Hensley, Smith, Kline & Beechem Labs. (United States)
Jay R. Knutson, National Institutes of Health (United States)

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

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