Bulletin of the American Physical Society
APS March Meeting 2011
Volume 56, Number 1
Monday–Friday, March 21–25, 2011; Dallas, Texas
Abstract: S1.00123 : Time-resolved infrared structural biology: from active-site structural dynamics to proton transfer mechanism of photoactive yellow protein
Author:
Proton transfer is a fundamental process in biology. We employ photoactive
yellow protein (PYP), a bacterial blue light receptor protein, as an ideal
model system to study the physical mechanism of intra-molecular proton
transfer in proteins. We employ time-resolved step-scan FTIR spectroscopy to
detect functionally important structural changes in the active site of PYP
before and after proton transfer from Glu46 to the negatively charged
phenolic group of the $p$-coumaric acid chromophore in PYP, which occurs on a
250 microsecond time scale. In addition, we employ a combination of isotope
editing and site-specific mutations to identify the vibrational modes and
structural origins of infrared signals, and we develop and utilize
vibrational structural markers to translate infrared signals to structural
information. We will demonstrate the power of time-resolved infrared
structural biology in structure-function studies of proteins and in proton
transfer mechanism in photoactive yellow protein.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2011.MAR.S1.123
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