00655nas a2200229 4500008004100000020001400041245004500055210004500100300000900145490000700154100002600161700001700187700002100204700002100225700003300246700002100279700001700300700001600317700002000333700002300353856004900376 2019 eng d a2041-172300aProtein and RNA dynamical fingerprinting0 aProtein and RNA dynamical fingerprinting a1-100 v101 aNiessen, Katherine, A1 aXu, Mengyang1 aGeorge, Deepu, K1 aChen, Michael, C1 aFerré-D’Amaré, Adrian, R1 aSnell, Edward, H1 aCody, Vivian1 aPace, James1 aSchmidt, Marius1 aMarkelz, Andrea, G uhttps://markelz.physics.buffalo.edu/node/19902250nas a2200157 4500008004100000245009400041210006900135260001700204520170800221100001801929700001701947700002701964700002001991700002402011856005702035 2016 eng d00aDirect Measurements of the Long-Range Collective Vibrations of Photoactive Yellow Protein0 aDirect Measurements of the LongRange Collective Vibrations of Ph aBaltimore MD3 a

Long-range collective vibrations are thought to be crucial to protein functions. In the case of photoactive protein family, modeling suggests the intramolecular vibrations provide an efficient means of energy relaxation[1], feedback for enhancement of chromophore vibrations that promote structural transitions[2] and can assist in charge energy transfer[3]. As a paradigm of this family, photoactive yellow protein (PYP) is a cytoplasmic photocycling protein related to negative phototactic response to blue light in purple photosynthetic bacteria. PYP has a p-coumaric acid chromophore binding to the cysteine residue via a thioester bond, whose vibrations were found to overlap calculated vibrations of the protein scaffold. Using our unique technique of anisotropic terahertz microscopy(ATM)[4], we measure the intramolecular vibrations for PYP for the first time, including cycling between ground and blue shift (pB) states. Room temperature ATM measurements are performed in the dark and with continuous wave illumination at 488nm, resulting in a steady pB state with approximately 5% population conversion. In pB state, we find an overall decrease in the strength of resonant band in frequency range of 30-60 cm-1. Our calculated spectra using quasi-harmonic analysis indicate that our measurements are dominated by the protein vibrations, rather than the pCA chromophore, allowing us to characterize how the scaffold dynamics changes with functional states and mutations.

1. Levantino, M., et al. Nat Commun, 2015. 6.

2. Mataga, N., et al. Chem. Phys. Lett., 2002. 352(3-4): p. 220-225.

3. Fokas, A.S., et al. Photosynth. Res., 2014. 122

1 aDeng, Yanting1 aXu, Mengyang1 aNiessen, Katherine, A.1 aSchmidt, Marius1 aMarkelz, Andrea, G. uhttps://onlinelibrary.wiley.com/doi/10.1002/pro.3026