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Full-Text Articles in Physics

Charge Transfer Assisted By Collective H-Bonding Network Dynamics, Omar F. Mohammed, Christina M. Othon, Oh-Hoon Kwon, Ahmed H. Zewail Jul 2009

Charge Transfer Assisted By Collective H-Bonding Network Dynamics, Omar F. Mohammed, Christina M. Othon, Oh-Hoon Kwon, Ahmed H. Zewail

Christina M Othon

Although there have been numerous studies of solvation, the role of solvent specific and collective interactions, especially for charge-transfer processes, remains difficult to unravel. Here, we report, using femtosecond fluorescence up-conversion and steady-state spectroscopic measurements, studies of well-designed single-sited formylperylene (FPe) in binary solvents. One of the solvents (methanol, MOH) can selectively hydrogen (H) bond to the carbonyl (C=O) site, while the other (acetonitrile, ACN) cannot, but both have similar polarity ( for MOH and for ACN). The results reveal that ultrafast charge transfer from the perylene unit to the carbonyl group of FPe is facilitated by site-specific H-bonding interactions …


Solvation In Protein (Un)Folding: Effect Of Local And Bulk Dynamics In The Melittin Tetramer-Monomer Transition, Christina M. Othon, Oh-Hoon Kwon, Milo M. Lin, Ahmed H. Zewail May 2009

Solvation In Protein (Un)Folding: Effect Of Local And Bulk Dynamics In The Melittin Tetramer-Monomer Transition, Christina M. Othon, Oh-Hoon Kwon, Milo M. Lin, Ahmed H. Zewail

Christina M Othon

Protein structural integrity and flexibility are intimately tied to solvation. Here we examine the effect that changes in bulk and local solvent properties have on protein structure and stability. We observe the change in solvation of an unfolding of the protein model, melittin, in the presence of a denaturant, trifluoroethanol. The peptide system displays a well defined transition in that the tetramer unfolds without disrupting the secondary or tertiary structure. In the absence of local structural perturbation, we are able to reveal exclusively the role of solvation dynamics in protein structure stabilization and the (un)folding pathway. A sudden retardation in …


Alamethicin In Lipid Bilayers: Combined Use Of X-Ray Scattering And Md Simulations, Jianjun Pan, D. Peter Tieleman, John F. Nagle, Norbert Kučerka, Prof. Stephanie Tristram-Nagle Ph.D. Dec 2008

Alamethicin In Lipid Bilayers: Combined Use Of X-Ray Scattering And Md Simulations, Jianjun Pan, D. Peter Tieleman, John F. Nagle, Norbert Kučerka, Prof. Stephanie Tristram-Nagle Ph.D.

Prof. Stephanie Tristram-Nagle Ph.D.

We study fully hydrated bilayers of two di-monounsaturated phospholipids diC18:1PC (DOPC) and diC22:1PC with varying amounts of alamethicin (Alm). We combine the use of X-ray diffuse scattering and molecular dynamics simulations to determine the orientation of alamethicin in model lipids. Comparison of the experimental and simulated form factors shows that Alm helices are inserted transmembrane at high humidity and high concentrations, in agreement with earlier results. The X-ray scattering data and the MD simulations agree that membrane thickness changes very little up to 1/10 Alm/ DOPC. In contrast, the X-ray data indicate that the thicker diC22:1PC membrane thins with added …