The research is aimed at characterizing the responses of various media to optically triggered events. The triggering involves electronic excitation, electron transfer, photochemical reaction and ligand release. The various media include model solvents and proteins. The specific goal is to learn how proteins respond to changes in the structure or charge distribution of chromophores imbedded in them or to charge separation. The novel method of transient infrared spectroscopy will be used in order that the vibrational frequencies and dynamics of the equilibrium distribution can be evaluated. Specifically, experiments will be carried out on electron transfer processes in reaction centers from photosynthetic bacteria and model systems in which the incoherent and coherent responses will be explored. Ligand release experiments on hemoglobin and myoglobin are planned to investigate the resulting protein conformational change. Also the structural responses of the 'de novo' synthesized proteins will be studied by infrared methods. Efforts are underway to devise new methods of understanding the IR spectra of proteins using hole burning.

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National Institute of General Medical Sciences (NIGMS)
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University of Pennsylvania
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Fry, Bryan A; Solomon, Lee A; Leslie Dutton, P et al. (2016) Design and engineering of a man-made diffusive electron-transport protein. Biochim Biophys Acta 1857:513-521
Goparaju, Geetha; Fry, Bryan A; Chobot, Sarah E et al. (2016) First principles design of a core bioenergetic transmembrane electron-transfer protein. Biochim Biophys Acta 1857:503-512
Sharp, Kim A; Vanderkooi, Jane M (2010) Water in the half shell: structure of water, focusing on angular structure and solvation. Acc Chem Res 43:231-9
Zelent, Bogumil; Sharp, Kim A; Vanderkooi, Jane M (2010) Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH. Biochim Biophys Acta 1804:1508-15
Coleman, Ryan G; Sharp, Kim A (2010) Shape and evolution of thermostable protein structure. Proteins 78:420-33
Coleman, Ryan G; Sharp, Kim A (2010) Protein pockets: inventory, shape, and comparison. J Chem Inf Model 50:589-603
Zelent, B; Vanderkooi, J M (2009) Infrared spectroscopy used to study ice formation: the effect of trehalose, maltose, and glucose on melting. Anal Biochem 390:215-7
Coleman, Ryan G; Sharp, Kim A (2009) Finding and characterizing tunnels in macromolecules with application to ion channels and pores. Biophys J 96:632-45
Zelent, Bogumil; Vanderkooi, Jane M; Nucci, Nathaniel V et al. (2009) Phosphate assisted proton transfer in water and sugar glasses: a study using fluorescence of pyrene-1-carboxylate and IR spectroscopy. J Fluoresc 19:21-31
Frederick, Kendra King; Sharp, Kim A; Warischalk, Nicholas et al. (2008) Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation. J Phys Chem B 112:12095-103

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