Microfluidic mixers for studying protein folding

Journal of Visualized Experiments

Volumn , Issue 62, 2012, Pages

  Waldauer, Steven A ^a   Wu, Ling ^a   Yao, Shuhuai ^b   Bakajin, Olgica ^c   Lapidus, Lisa J ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Bioengineering; Fluorescence; FRET; Issue 62; Laminar flow; Microfluidic mixing; Protein folding

Indexed keywords

EID: 84860666242     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/3976     Document Type: Article

References (16)

1. Eaton, W.A., et al. Fast kinetics and mechanisms in protein folding. Annual Review of Biophysics and Biomolecular Structure. 29, 327-359 (2000).
2. Hertzog, D.E., et al. Femtomole mixer for microsecond kinetic studies of protein folding. Analytical Chemistry. 76, 7169-7178 (2004).
3. Hertzog, D.E., Ivorra, B., Mohammadi, B., Bakajin, O., & Santiago, J.G. Optimization of a microfluidic mixer for studying protein folding kinetics. Analytical Chemistry. 78, 4299-4306 (2006).
4. Yao, S. & Bakajin, O. Improvements in Mixing Time and Mixing Uniformity in Devices Designed for Studies of Protein Folding Kinetics. Analytical Chemistry. 79, 5753-5759 (2007).
5. Lapidus, L.J., et al. Protein Hydrophobic Collapse and Early Folding Steps Observed in a Microfluidic Mixer. Biophysical Journal. 93, 218-224 (2007).
6. Bilsel, O., Kayatekin, C., Wallace, L.A., & Matthews, C.R. A microchannel solution mixer for studying microsecond protein folding reactions. Review of Scientific Instruments. 76, (2005).
7. Chan, C.-K., et al. Submillisecond protein folding kinetics studied by ultrarapid mixing. PNAS. 94, 1779-1784 (1997).
8. Shastry, M.C.R., Luck, S.D., & Roder, H. A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophysical Journal. 74, 2714-2721 (1998).
9. Pollack, L., et al. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proceedings of the National Academy of Sciences of the United States of America. 96, 10115-10117 (1999).
10. Takahashi, S., et al. Folding of cytochrome c initiated by submillisecond mixing. Nature Structural Molecular Biology. 4, 44-50 (1997).
11. Knight, J.B., Vishwanath, A., Brody, J.P., & Austin, R.H. Hydrodynamic focusing on a silicon chip: Mixing nanoliters in microseconds. Physical Review Letters. 80, 3863-3866 (1998).
12. DeCamp, S.J., Naganathan, A.N., Waldauer, S.A., Bakajin, O., & Lapidus, L.J. Direct Observation of Downhill Folding of lambda-Repressor in a Microfluidic Mixer. Biophysical Journal. 97, 1772-1777 (2009).
13. Waldauer, S.A., et al. Ruggedness in the folding landscape of protein L. Hfsp Journal. 2, 388-395 (2008).
14. Shastry, M.C.R. & Roder, H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Structural Biology. 5, 385-392 (1998).
15. Uzawa, T., et al. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness. Proceedings of the National Academy of Sciences of the United States of America. 101, 1171-1176 (2004).
16. Zhu, L., et al. Evidence of Multiple Folding Pathways for the Villin Headpiece Subdomain. The Journal of Physical Chemistry B. 115, 12632-12637 (2011).