Advanced Infrared Biology of Protein Structure & Dynamics
ORAL
Abstract
Proton-transfer in protein is a fundamental process underlying a range of protein functions. Study of proton transfer and its role in protein function is seriously hampered due to lack of widely accessible structural techniques. To overcome this barrier, we develop time-resolved infrared vibrational spectroscopy-based technology enhanced by amino-acid specific isotope editing and site-specific mutations using photoactive yellow protein (PYP) as the “hydrogen atom” of proteins. We will report development and applications of this advanced Fourier transform infrared (FT-IR) technology to photoactive yellow protein, a blue light photoreceptor protein. Three strategically designed mutants of PYP, namely H3Q PYP, H108 PYP, and E46Q PYP are used in this study, as well as 15N isotope edited histidine.
*"This work was supported by the National Institutes of Health (NIH) under award R15GM144898-01 and the supplement grant 3R15GM144898-01S1, and by the National Science Foundation (NSF) under award DBI 1338097
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Publication: Planned paper: Developing an experimental method for detection of proton transfer during protein function.
Presenters
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Aihua Xie
- Oklahoma State University-Stillwater