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Proceedings Paper

Rapid events in protein folding studied by laser-induced pH and temperature jumps
Author(s): Anne Gershenson; Christopher J. Fischer; Joseph A. Schauerte; Duncan G. Steel; Ari Gafni
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Paper Abstract

Traditional methods, such as stopped flow, used to study early events in protein folding are limited, by instrument dead times, to investigating events which occur milliseconds after the initiation of folding. We have developed a laser-based temperature jump apparatus capable of measuring changes in the fluorescence of proteins undergoing folding or unfolding on the microsecond timescale following a laser-induced pH, or temperature, jump. The development of the system is discussed and the results for experiments with RNase T1 and Apomyoglobin are summarized.

Paper Details

Date Published: 1 May 1998
PDF: 11 pages
Proc. SPIE 3256, Advances in Optical Biophysics, (1 May 1998); doi: 10.1117/12.307067
Show Author Affiliations
Anne Gershenson, Univ. of Michigan (United States)
Christopher J. Fischer, Univ. of Michigan (United States)
Joseph A. Schauerte, Univ. of Michigan (United States)
Duncan G. Steel, Univ. of Michigan (United States)
Ari Gafni, Univ. of Michigan (United States)


Published in SPIE Proceedings Vol. 3256:
Advances in Optical Biophysics
Joseph R. Lakowicz; J. B. Alexander Ross, Editor(s)

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