K. E. Laidig Curriculum Vitae

Keith E. Laidig, Ph. D.
Department of Biochemistry University of Washington Seattle, WA 98195-7610 E-Mail: laidig@u.washington.edu	Phones: (206) 660-6035 (Voice/Voice Mail) (206) 685-1792 (FAX)

Education:

Yale University, Ph. D Chemistry 1988

Advisors: K. B. Wiberg and M. Saunders

Thesis: Theoretical Investigation of I. Barriers to Rotation Adjacent to Carbonyl Groups in Carboxylic Acids and Esters and II. Structures, Energies, Modes of Interconversion, and Isotope Effects in the Cyclopropylcarbinyl-cyclobutyl and Bicyclo[2.1.1]hexyl Cations.

Yale University, M. S. Chemistry 1988
Yale University, M. Phil. Chemistry 1989
Carleton College, B.A. Chemistry 1984, with distinction.

Advisor: Charles H. Carlin

Thesis: Homoenolization: A Study of Mechanism.

Experience:

7/2000 - present, Howard Hughes Medical Institute Affiliate(System Administrator):

Department of Biochemistry, University of Washington, D. Baker

Manage Baker Group network and computing resources; a large heterogeneous environment (>1200 compute cores in 13 clusters, mutiple TB storage, Gb end-to-end VLAN network) distributed over 4 datacenters in the Seattle area). Some of the gear seen here {front view}. & back view}.

1/2000 - 6/2000, Computer Technician & Staff Scientist:

Study of symplectic and multiple time-step algorithms for ultra-long molecular dyanamics simulations. System administration and process optimization.

11/1998 - present, Consulting Companies:

Formix LLC - Secure Networking and High-Performance Computing

1/1998 - 11/1998, Research Associate:

Implementation of symplectic and multiple time-step algorithms for ultra-long molecular dyanamics simulations. Continued development of accurate mixed-solvent models for simulations. Continued studies of structure, dynamics, and stabilites of prion protein.

1/1997 -12/1997, Research Associate:

Development of accurate mixed-solvent models for simulations. Development of computational tools to study solvent dynamics and interaction with proteins. Studies of structure, dynamics, and stabilites of prion protein.

1/1994 - 12/1996, Research Associate:

Department of Medicinal Chemistry, University of Washington, V. Daggett

Molecular dynamics simulation of folding intermediates of ferricytochrome b562. Studies of hydrophobic hydration. Investigation of atomic and functional group origins of linear and non-linear polarizabilities.

10/1992- 11/1993, Postdoctoral Fellow:

College of Chemistry, University of California, Berkeley, A. Streitwieser

Development and studies of the localization of electron pairs in unsaturated and conjugated systems using the Fermi hole. Studies of the atomic and functional group origins of relative acidity trends. Studies of homo- and hetero-solvent molecule dimers and cation-solvent complexes.

1/1991 - 9/1992, Research Associate:

Department of Theoretical Chemistry, University of Cambridge, R. D. Amos and N. C. Handy

Development and implementation of wavefunction analysis tools and frequency-dependent second hyperpolarizabilites within the CADPAC program package. Investigation of the atomic origins of molecular moments and polarizabilities. Characterization of atomic and molecular interaction within X-ray determined structures using properties of the experimental charge distributions.

9/1988 - 12/1990, Postdoctoral Fellow:

Department of Chemistry, McMaster University, R. F.W. Bader

Theoretical investigations of reaction pathways, barriers to rotation and inversion, and atomic and molecular polarizabilities. Development and implementation of electric field perturbation in order to extend the theory of atoms in molecules to include effects of electromagnetic fields. Reworking, simplification, and optimization of the atoms in molecules (AIMPAC) program suite.

6/1985 - 9/1988, Research Assistant:

Department of Chemistry, Yale University, M. Saunders and K. B. Wiberg

Theoretical studies of barriers to rotation in acids, esters, and amides. Studies of structure and reaction pathways in carbocationic systems. Development of techniques to calculate reduced isotopic partition function ratios for the investigation of equilibrium isotope effects.

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