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Femtomole Mixer for Microsecond Kinetic Studies of Protein Folding

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David E. Hertzog,^†^‡ Xavier Michalet,^§ Marcus Jäger,^§ Xiangxu Kong,^§ Juan G. Santiago,^† Shimon Weiss,^§ and Olgica Bakajin*^‡

Mechanical Engineering Department, Stanford University, Stanford, California 94305, Department of Chemistry and Materials Science, Lawrence Livermore National Laboratory, Livermore, California 94550, and Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California 90095

Anal. Chem., 2004, 76 (24), pp 7169–7178

DOI: 10.1021/ac048661s

Publication Date (Web): November 13, 2004

Section:

Biochemical Methods

Abstract

We have developed a microfluidic mixer for studying protein folding and other reactions with a mixing time of 8 μs and sample consumption of femtomoles. This device enables us to access conformational changes under conditions far from equilibrium and at previously inaccessible time scales. In this paper, we discuss the design and optimization of the mixer using modeling of convective diffusion phenomena and a characterization of the mixer performance using microparticle image velocimetry, dye quenching, and Förster resonance energy-transfer (FRET) measurements of single-stranded DNA. We also demonstrate the feasibility of measuring fast protein folding kinetics using FRET with acyl-CoA binding protein.

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This article has been cited by 15 ACS Journal articles (5 most recent appear below).

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Microfluidic Mixers for the Investigation of Rapid Protein Folding Kinetics Using Synchrotron Radiation Circular Dichroism Spectroscopy
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Improvements in Mixing Time and Mixing Uniformity in Devices Designed for Studies of Protein Folding Kinetics
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  Using a microfluidic laminar flow mixer designed for studies of protein folding kinetics, we demonstrate a mixing time of 1 ± 1 μs with sample consumption on the order of femtomoles. We recognize two limitations of previously proposed designs: (1) size ...
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