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Protein Science (2004), 13:2578-2587. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Characterizing specific phage–protein interactions by fluorescence correlation spectroscopy

John T. Bahns, Chin-Mei Liu and Liaohai Chen

Biosciences Division, Argonne National Laboratory, Argonne, Illinois 60439, USA

(RECEIVED February 12, 2004; FINAL REVISION June 3, 2004; ACCEPTED July 2, 2004)

The interactions of several affinity reagent displayed T7 and M13 phage particles with their corresponding target molecules were examined using Fluorescence Correlation Spectroscopy (FCS). Diffusion times, relative fractions of each component in the recognition reactions at the equilibrium state, and ultimately the dissociation constants were deduced from analyzing the fluorescence autocorrelation curves. Although the sample preparation and FCS characterization of icosahedral T7-related systems were relatively straight forward, procedures with filamentous M13-related systems were complicated by the physical size of M13 and its aggregate formation. Methods that accommodate the FCS measurement of the M13 phage via changing confocal optics, fitting procedures, and aggregate discrimination are presented and discussed.

Keywords: phage–protein interaction; phage display; combinational libraries; M13 phage; T7 phage; fluorescence correlation spectroscopy; dissociation constants

Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04695704.

Reprint requests to: Liaohai Chen, Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA; e-mail: lhchen{at}anl.gov; fax: (630) 252-5517.


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