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Dr. Philip Anfinrud
Senior Biomedical
Research Scientist
Laboratory of Chemical Physics
NIH, National Institute of Diabetes and
Digestive and Kidney Diseases

Researcher Views Protein's Structural Changes in Real Time Utilizing X-ray Crystallography

Dramatic structural changes that take place inside a protein in less than a billionth of a second have been filmed in high resolution utilizing picosecond X-ray crystallography, enabling scientists to view atom-scale movies.(1)

Previous x-ray movies of proteins have been on the nanosecond time scale, which is too slow for capturing the steps of many protein processes.  The ability to watch a protein functioning on the inside may lead to a better understanding of how it works, enabling scientists to engineer improved proteins for blood substitutes and improved treatments for genetic diseases.(1)

A leader in this field, Philip Anfinrud, Senior Biomedical Research Scientist in the Laboratory of Chemical Physics at the NIH's National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) will spend a week at Cornell University, September 12-16, 2005 to discuss his research and techniques as the Frontier Applications in Synchrotron Radiation Guest Lecturer.

Anfinrud will give two lectures during his week long stay, the first entitled, "Watching Proteins fFunction in Real Time with Picosecond Time-resolved X-ray Crystallography," will be at 4:30 pm in 119 Baker on Tuesday, September 13, 2005 with a reception beginning at 4:00 p.m.  Dr. Anfinrud will discuss his recent research on Myoglobin, a ligand-binding heme protein found in our muscle tissue.  Flash photolysis of the carbon monoxide adduct liberates CO from the heme binding site, promptly producing a well-defined reactive state.  Anfinrud has used time-resolved X-ray crystallography to probe the time-dependent structural changes that ensue upon ligand dissociation.  Three-dimensional "snapshots" of the protein structure have been stitched together into movies that unveil protein motion in real time.  The mechanistic insights gained by literally watching proteins as they execute their designed function will help pave the way to harness the amazing capabilities of these nanoscale molecular machines.

The second lecture in the series will be of a more technical nature entitled "How Do Proteins Work?  Unveiling Functional Mechanisms with Femtosecond IR Spectroscopy, Picosecond X-ray Crystallography, and Molecular Dynamics Simulations."  This lecture will be held on Thursday, September 15, 2005 at 4:30 pm in 119 Baker with a reception beginning at 4:00 p.m.  Dr. Anfinrud will focus on recent developments of picosecond time-resolved X-ray crystallography which has allowed his group to visualize in real time and with atomic detail the conformational evolution of a protein.  Showing how the unique combination of simulation and experiment unveils, at an atomic level, relationships among protein structure, dynamics and function.

The Frontier Applications in Synchrotron Radiation Lecture Series, is free and open to the public.  This series was established by the Cornell High Energy Synchrotron Source and Provost Biddy Martin, which highlights pioneering scientists who are utilizing synchrotron radiation in new directions, especially in the biological and environmental areas.

(1) Science Blog, June 2003