Faculty Research Interest

Structural Dynamics, Conformational Disorder, and Reactivity in Proteins: Laser Spectroscopic Studies

Faculty Record

The primary focus of Dr. Friedman's research program is to carry out an integrated investigation of structure, structural dynamics and function on protein samples both in solution and in unusual solid state matrices at both ambient and cryogenic temperatures. Laser probe techniques with time resolution capabilities starting at less than a trillionth of a second are used to provide atomic level resolution for both structural and functional properties.

The following projects are currently being pursued as part of Dr. Friedman's research program:

Hemoglobin and myoglobin. The overall objective of this project is to dissect out the structural and dynamical elements that control oxygen binding properties in these two model protein systems. Dr. Friedman is the Director of the AECOM Blood Substitute Program Project which seeks through a multidisciplinary effort to create acellular hemoglobin based blood substitutes for clinical use. Molecular biophysics is used in this program to help direct the chemical and mutagenic synthetic effort to create novel hemoglobin structures having the desired functional properties.

Ca binding sites in biological molecules. How divalent cations trigger biological activity is poorly understood on the molecular level. We have developed a new spectroscopic technique which provides detailed site specific structural and dynamical information from the molecular groups that comprise divalent cation binding sites in biological molecules including proteins, phospholipids and nucleic acids. The technique also allows for the direct study of water dynamics at specific metal binding sites in both proteins and membranes.

Structure-function studies on transferrin.

The use of sol-gel encapsulation techniques to trap and study non-equilibrium protein structures including folding and unfolding intermediates.