Paper
1 May 1990 Applications of KINDK: following macromolecular processes with lifetimes
Susan M. Green, Preston Hensley, Jay R. Knutson
Author Affiliations +
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).
© (1990) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Susan M. Green, Preston Hensley, and Jay R. Knutson "Applications of KINDK: following macromolecular processes with lifetimes", Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); https://doi.org/10.1117/12.17687
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KEYWORDS
Biochemistry

Proteins

Laser spectroscopy

Luminescence

Metals

Ions

Biological research

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