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Blasting antibodies with lasers provides direct way of measuring their flexibilities

ing," says Romesberg.

In their experiments, Romesberg and Jimenez mix human antibodies with dye molecules. When the mixture is blasted with the laser beam, the dye molecules absorb energy from the laser and transmit some of this energy into the antibody.

The only place for the energy to go within the antibody is for it to be absorbed by vibrating bonds within the protein. The electron distribution in these bonds may then change, depending on how much they vibrate. By comparing an excited, "spectra" readout to a normal spectrum, Romesberg and his colleagues can assess how flexible particular parts of a protein are.

This is not always simple. Antibodies are large proteins with lots of vibrating bonds, and molecular motions. Quantum mechanical calculations can help researchers delineate which motions are primary participants in the antibody-antigen recognition process. Baldridge took the results of these computations and provided a visual way to understand the effect of the force on the protein.

The quantum mechanical calculations actually give a depiction of the electrostatic processes that are occurring. Together with the experimental information, this helps complete the puzzle of how various bonds are moving, twisting, and interacting with other atoms in the protein environment.

The lock-and-key model specifies that if the antigen and antibody are not matched up in a rigid, structural way, they will not bind. Romesberg, Baldridge, and their colleagues found this to be true for one of the antibodies they tested. But two of the other antibodies appeared to wiggle a lot to achieve their optimal energetic state.

Antibody recognition, says Romesberg, may not be a simple, lock-and-key mechanism, but one in which the keys and the locks are vibrating and changing their shape as they come together in solution.


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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
17-Dec-2002


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