当前位置: X-MOL首页全球导师 海外导师 › Beck, Warren F.

个人简介

B.S., 1982, Davidson College Ph.D., 1988, Yale Univ. Miller Institute Postdoctoral Fellowship, 1989–91, Univ. of California, Berkeley Award Organization Division Level Code Type Code Start Date End Date Cottrell Scholars Award Research Corporation Professional Honors 1994 Teaching Fellowship Lilly Endowment Professional Fellowship 1993 1994 Searle Scholarship Chicago Community Trust/Searle Scholars Program Professional Honors 1992 1995 Miller Institute Postdoctoral Fellowship University of California, Berkeley Postdoctoral Fellowship 1989 1991 Ph.D. Yale University Graduate Degree 1988 Richard Wolfgang Dissertation Prize Yale University Department of Chemistry Graduate Honors 1988 Bachelor of Science Cum Laude Davidson College Undergraduate Degree 1982 Kent Fellowship Yale University Department of Chemistry Graduate Fellowship 1982 1986 Phi Beta Kappa Phi Beta Kappa Undergraduate Honors 1982 Graduate Fellowship National Science Foundation Graduate Fellowship 1982 1985 Date Content 01/06/2006 Warren Beck, Marcos Dantus, Michael Feig, John Frost, Jim Geiger, Ned Jackson, Rob Maleczka, Jim McCusker, Aaron Odom, Piotr Piecuch, Tom Pinnavaia, Greg Swain, and Bill Wulff received new grants during Fall 2005.

研究领域

Biological Chemical Physics Inorganic Physical

(Research Description PDF - 1100 kb) The Beck group uses femtosecond nonlinear spectroscopy to study photophysical and photochemical processes in photosynthetic light-harvesting proteins, protein dynamics in redox proteins, and model systems. The current focus is on how carotenoids function in energy transfer and photoprotection mechanisms in light-harvesting proteins. A second project examines the dynamics of water molecules in the hydration shell of proteins and the coupling of these motions to protein motions. Both areas exploit advanced two-dimensional photon-echo and transient-grating spectroscopies to characterize the formation and decay of electronic coherences and structural intermediates or to discern the motion of the surrounding protein or solvent medium. In the carotenoid project, the initial target is the peridinin–chlorophyll a protein, a light-harvesting protein from marine dinoflagellates that incorporates the carotenoid peridinin as its main light-absorbing chromophore. Energy absorbed from the mid-visible part of the solar spectrum by peridinin is transferred efficiently to chlorophyll a on the < 3 ps timescale. The project’s main goal is to understand the origin of the efficiency of this energy transfer channel. Transient-grating spectroscopy is being used to assess the formation of intermediates with charge-transfer character in the radiationless decay of the resonant S2 (1 1Bu+) state and to detect double-quantum coherences. Two-dimensional spectroscopy is being used to determine how these intermediates function in energy transfer to chlorophyll a. In the hydration shell project, we are studying how the solvent surroundings of proteins plays a role in the stability and dynamics of a folded protein. The hydration shell of proteins is a ~10 ? thick layer of polarized water molecules that interacts strongly with charges on the surface of the protein so that the motions of the water and protein are coupled. Transient grating spectroscopy and two-dimensional spectroscopy are being used in this project with electronic probes that are positioned in the hydration shell. Our findings indicate that the dynamics of water in the hydration shell is much different from that in bulk water, perhaps owing to the formation of hydrogen-bonded chains. Left: Trimeric complex of the peridinin–chlorophyll a protein from Amphidinium carterae (1PPR.pdb). Right: Space-filling rendering of the chromophores in a single subunit: peridinin (magenta) and chlorophyll a (yellow). Lower right: structure of peridinin. Femtosecond two-dimensional spectroscopy using spectral interferometry: A) stimulated photon-echo pulse sequence; B) spectral interferogram; C) Fourier transform of spectral interferogram; D) third-order spectrum after windowing in the time domain.

近期论文

查看导师新发文章 (温馨提示:请注意重名现象,建议点开原文通过作者单位确认)

Posey, L. A.; Hendricks, R. J.; Beck, W. F. Dynamic Stokes shift of the time-resolved phosphorescence spectrum of ZnII-substituted cytochrome c. J. Phys. Chem. B 2013, 15926–15934. Tripathy, J.; Mueller, J. J.; Shepherd, N. C.; Beck, W. F. Dynamic solvation and coupling of the hydration shell of ZnII-substituted cytochrome c in the presence of guanidinium ions. J. Phys. Chem. B 2013, 14589-14598. Dillman, K. L.; Beck, W. F. Vibrational coherence from van der Waals modes in the native and molten-globule states of ZnII-substituted cytochrome c. J. Phys. Chem. B 2011, 115, 8657–8666. Tripathy, J.; Beck, W. F. Nanosecond-regime correlation timescales for equilibrium protein structural fluctuations of metal-free cytochrome c from picosecond time-resolved fluorescence spectroscopy and the dynamic Stokes shift. J. Phys. Chem. B 2010, 114, 15958–15968. Dillman, K. L.; Beck, W. F. Excited-state vibrational coherence in methanol solution of ZnII tetrakis (N‑methylpyridyl) porphyrin: charge-dependent intermolecular mode frequencies and implications for electron-transfer dynamics in photosynthetic reaction centers. J. Phys. Chem. B. 2010, 114, 15269–15277. Dillman, K. L.; Shelly, K. R.; Beck, W. F. Vibrational coherence in polar solutions of ZnII tetrakis (N‑methylpyridyl) porphyrin with Soret-band excitation: rapidly damped intermolecular modes with clustered solvent molecules and slowly damped intramolecular modes from the porphyrin macrocycle. J. Phys. Chem. B 2009, 113, 6127–6139. Barns, K. J.; Lampa-Pastirk, S.; Dillman, K. L.; Wegener, A. J.; Beck, W. F. Intramolecular vibrational excitation of unfolding reactions in ZnII-substituted and metal-free cytochromes c: activation enthalpies from integrated fluorescence Stokes shift and lineshape excitation profiles. J. Phys. Chem. B 2008, 112, 15108–15115. Shelly, K. R.; Golovich, E. C., Dillman, K. L., and Beck, W. F. Intermolecular vibrational coherence in the bacteriochlorophyll proteins B777 and B820 from Rhodospirillum rubrum. J. Phys. Chem. B 2008, 112, 1299–1307. Lampa-Pastirk, S.; Beck, W. F. Intramolecular vibrational preparation of the unfolding transition state of Zn(II)-substituted cytochrome c. J. Phys. Chem. B 2006, 110, 22971–22974. Featured as the cover article for the 23 November 2006 issue. Shelly, K. R.; Golovich, E. C.; Beck, W. F. Intermolecular vibrational coherence in bacteriochlorophyll a with clustered polar solvent molecules. J. Phys. Chem. B 2006, 110, 20586–20595. Lampa-Pastirk, S.; Beck, W. F. Polar solvation dynamics in Zn(II)-substituted cytochrome c: diffusive sampling of the energy landscape in the hydrophobic core and solvent-contact layer. J. Phys. Chem. B 2004, 108, 16288–16294. Lampa-Pastirk, S.; Lafuente, R. C.; Beck, W. F. Excited-state axial-ligand photodissociation and nonpolar protein-matrix reorganization in Zn(II)-substituted cytochrome c. J. Phys. Chem. B 2004, 108, 12602–12607. Carson, E. A.; Diffey, W. M.; Shelly, K. R.; Lampa-Pastirk, S.; Dillman, K. L.; Schleicher, J. M.; Beck, W. F. Dynamic-absorption spectral contours: vibrational phase-dependent resolution of low-frequency coherent wave-packet motion of IR144 on the ground-state and excited-state π→π* surfaces. J. Phys. Chem. A 2004, 108, 1489–1500. Shelly, K. R.; Carson, E. A.; Beck, W. F. Vibrational coherence from the dipyridine complex of bacteriochlorophyll a: intramolecular modes in the 10–220-cm-1 regime, intermolecular solvent modes, and relevance to photosynthesis. J. Am. Chem. Soc. 2003, 125, 11810–11811. Beck, W. F. Ultrafast Spectroscopy. In Encyclopedia of Chemical Physics and Physical Chemistry; Moore, J. H., Spencer, N. D., Eds.; Institute of Physics Publishing, Ltd.: Bristol, England, 2001; Volume II, pp 1743–1772.

推荐链接
down
wechat
bug