PNNL Team Captures Individual Protein Interactions

Scientists at the Pacific Northwest National Laboratory in Richland, Wash., have used an established technique to observe real-time interactions between single protein molecules for the first time.

Written byAileen Constans

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includes residues 201 to 321 of WASP, which contains the CRIB domain essential for Cdc42 binding. (Reprinted with permission from P. Nalbant, Science, 305:1615–9, 2004.)

Scientists at the Pacific Northwest National Laboratory in Richland, Wash., have used an established technique to observe real-time interactions between single protein molecules for the first time. Ultimately, the PNNL method – single-molecule photon stamping spectroscopy – will be used to study signaling events in living cells. At present it offers more information about protein-protein interaction dynamics than can be obtained with conventional structural biology techniques such as nuclear magnetic resonance (NMR) and X-ray crystallography.

"Protein conformation fluctuation dynamics is a stochastic process," says lead investigator H. Peter Lu, a staff scientist at PNNL. "Experimentally you have to study this process under physiological conditions, and to be able to follow [it] one molecule at a time, otherwise those stochastic fluctuations will be ...

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