Fayer Lab Home Page

Fayer Lab Home Page

Research Director:

Michael D. Fayer

Keck 113

Department of Chemistry

Stanford University

Stanford, CA 94305-5080

Tel: (650) 723-4446

Fax: (650) 723-4817

E-mail: fayer@stanford.edu

wonderfest talk: pdf download

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Group Administrative Assistant:

Dewi Fernandez

Tel: (650) 725-3530

Fax: (650) 725-0259

E-mail: dewif@stanford.edu

Quantum Mechanics Book
Elements of Quantum Mechanics
Errata and Addenda

Group Meeting Schedule

Research Interests

Dynamics in Complex Liquids
Jie Li

We are investigating a variety of complex liquids in which the nature of the intermolecular interactions strongly influences both the structure and the dynamics of the liquids. Examples of such liquids are supercooled liquids, liquid crystals, polymer melts and polymers in solution. Using Heterodyne Detected Optical Kerr Effect (HOKE) experiment, we can study the dynamics in complex liquids from 50fs up to 1ms, which cross over from microscopic timescale to macroscopic time scale. This unique system opens us a door to the understanding of many mysteries, for instance, glass transition and nematic-isotropic transition in liquid crystal.

Water Dynamics in Nanoscopic Environments
Ivan Piletic, David Moilanen and David Ben Spry

Water is ubiquitous in nature and as a result frequently occurs in confined environments with nanometer sizes. The properties of water in such environments are observed to change quite dramatically when compared to bulk water. Nanoscopically confined water is important in chemistry, biology, geology, and materials. An example of a confined environment is a reverse micelle (inverted micelle with a nanoscopic water pool inside). We conduct ultrafast vibrational echo and pump-probe spectroscopies to examine the behavior of water confined in reverse micelles, pores in artificial membranes, and other systems of nanoscopic dimensions. The results are demonstrating substantial changes in the hydrogen bond network dynamics as well as marked differences in the orientational dynamics of water molecules. To what extent do interactions with the confining environment affect water molecules? More complex environments are involved in the solvation of large biological molecules (i.e. proteins). Water confined in cavities as well as around large proteins is suspected to exhibit dynamical characteristics distinct from bulk water, which may affect the function of a protein. These issues of interest and importance are currently being pursued within the broad scope of exploring the hydrogen bond dynamics of associated liquids.

Ultrafast Chemical Exchange Spectroscopy
Junrong Zheng and Kyungwon Kwak

See the C&E news summary of this project

Ultrafast infrared 2D vibrational echo spectroscopy (2D VES) is coherent vibrational spectroscopic technique that is akin to 2D NMR, but it operates on time scales as fast as 100 fs that are 9 orders of magnitude faster than typical NMR experiments. Because it is a type of vibrational spectroscopy, 2D VES directly examines the structural degrees of freedom of molecules and molecular systems, and, therefore, it is can examine in real time structural evolution of chemical systems. We are applying it to problems such as chemical exchange in which solute-solvent complexes are formed and dissociate, molecular isomerization, proton and electron transfer. In addition 2D VES is being used to study the dynamic interactions of solutes with solvents in liquids and supercritical fluids. It is also being applied to the study of hydrogen bond dynamics.

Dynamics in Biological Systems
Ilya Finkelstein and Aaron Massari

Proteins are large structurally dynamic molecules. Nature has learned to harness subtle structural fluctuations in accomplishing vital biological functions. Until recently, there were few tools available that could report on global protein fluctuations on the ultrafast timescales on which small subsections of a protein move. We are developing ultrafast multidimensional infrared spectroscopic methods and using these techniques to study protein dynamics in an entirely new manner.

We excite isolated vibrations within the protein. By watching these vibrations in real time we study the mechanisms that influence fast dynamics in proteins and the early stages of global structural evolution. In collaboration with theoreticians, we are gaining an atomic level understanding of the interplay between protein dynamics and its environment.

Dynamics of Photoinduced Electron Transfer and Geminate Recombination in Liquids and Micelles
Ksenia D. Glusac and Alexei A. Goun

The electron transfer process in freely diffusing systems is a complex phenomenon that requires careful statistical mechanical description of diffusive motion of donor-acceptor pairs coupled to the electron transfer reaction. Our group has developed experimental and theoretical techniques that allow us to extract the properties of reacting species and media around them. Using femtosecond pump-probe spectroscopy, we measure the kinetics of the photoinduced electron transfer and geminate recombination. The theoretical model includes the topology of the medium, the distance dependence of the transfer rate, diffusion, and other factors necessary for a realistic description. The combination of experiment and theory allows us to obtain the parameters, such as donor/acceptor coupling constants, dielectric properties of the solvent, the escape probability for the radicals. This study is essential for the correct description of photovoltaic devices.