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Proceedings Paper

Exploring the conformational space of FRET biosensors for improved designs
Author(s): Kevin Truong; Elizabeth Pham
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Paper Abstract

Fusion proteins are an important class of proteins with diverse applications in biotechnology. They consist of 2 or more rigid domains joined by a flexible linker. Understanding the conformational space of fusion proteins conferred by the flexible linkers is important to predicting its behavior. In this paper, we introduce a modeling tool called FPMOD (Fusion Protein MODeller) which samples the conformational space of fusion proteins by treating all domains as rigid bodies and rotating each of them around their flexible linkers. As a demonstration, FPMOD was used to predict the fluorescence resonance energy transfer (FRET) efficiency of three different fusion protein biosensors. The simulation results of the FRET efficiency prediction were consistent with the in vitro experimental data, which verified that FPMOD is a valid tool to predicting the behavior of fusion proteins.

Paper Details

Date Published: 29 February 2008
PDF: 8 pages
Proc. SPIE 6868, Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes, 686806 (29 February 2008); doi: 10.1117/12.763634
Show Author Affiliations
Kevin Truong, Univ. of Toronto (Canada)
Institute of Biomaterials and Biomedical Engineering, Univ. of Toronto (Canada)
Elizabeth Pham, Institute of Biomaterials and Biomedical Engineering, Univ. of Toronto (Canada)


Published in SPIE Proceedings Vol. 6868:
Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes
Alexander P. Savitsky; Robert E. Campbell; Robert M. Hoffman, Editor(s)

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