X-Ray Crystallography

Crystallography provides a direct approach for obtaining high resolution molecular structures of biological macromolecules with virtually no limitations on molecular size. Both soluble macromolecules and membrane proteins can be studied by this technique. Research at Stony Brook currently focuses on DNA repair processes and the catalytic mechanisms of metalloenzymes and metallo cofactor biosynthesis. Research interests also include proteins which play essential roles in cellular regulation and signal transduction.

NMR Spectroscopy

Multidimensional NMR spectroscopy provides a versatile approach for obtaining high resolution structures of biological macromolecules in solution and membrane environments. High resolution structures can be obtained of proteins, DNA, RNA and their complexes in solution using traditional methods and of membrane proteins using magic angle spinning techniques. Besides structural information, NMR techniques can be used to measure the rates and amplitudes of molecular motions. Research using solution NMR spectroscopy is underway in the area of protein folding and DNA-protein recognition. Research using solid-state NMR spectroscopy focuses on the structure of membrane receptors and ion channels.

Computational Biology

Computational approaches and molecular graphics are an intrinsic component of structural biology. Both crystallography and NMR spectroscopy rely on computational strategies for model building and the refinement of molecular structures. Active areas of research at Stony Brook use molecular dynamics simulations to model atomic trajectories over short time scales and use electrostatic calculations to estimate the energetics of binding and insertion of proteins into biological membranes.

Biophysical Approaches

At the heart of structural biology is the correlation of structure and function. Such correlations rely on biophysical approaches for measuring binding constants, reaction rates, and the structural changes of key catalytic groups. Time resolved structural measurements can be made by fluorescence, infrared, Raman and absorption spectroscopy using facilities in research laboratories at Stony Brook, as well as Laue crystallography utilizing synchrotron radiation at the Brookhaven National Laboratory. Biophysical methods are critical for studies of protein folding, enzyme reaction mechanisms and low resolution structure analysis.