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Biophysical Society Meeting: From pores to spiders

Nathan Blow

From the expanding use of atomic force microscopy to growing interest in applying single-molecule FRET, the 2010 Biophysical Society annual meeting highlighted new tools and techniques for probing the physical and chemical interactions, forces, and functions underlying biological systems and processes.

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This week, over 6000 scientists descended upon San Francisco to take part in the 54th annual meeting of the Biophysical Society. The four-day event covered a diverse range of scientific topics, and highlighted the emergence of new tools and techniques for probing the physical and chemical interactions, forces, and functions underlying numerous biological systems and processes. From the expanding use of atomic force microscopy (AFM) and optical traps to growing interest in applying single-molecule FRET and super resolution imaging, it is clear that the dissemination of sophisticated tools is happening fast and allowing more and more biophysicists to explore the cellular world in previously unimaginable ways.

Deciphering large protein complexes

Large protein complexes, such as the nuclear pore complex, remain difficult to isolate and decode owing to the large number of protein constituents. In a session focused on deciphering these complexes, Carol Robinson from the University of Oxford talked about the use of mass spectrometry as one tool now being applied to tackle these structures. But in her talk, Robinson noted the need to use not only traditional structure determination approaches—such as NMR, computational modeling, and X-ray—but to also combine these data with mass spectrometry and other emerging methods to obtain integrated structural datasets that can be used together to obtain higher resolution structural understanding of these large complexes.

Nanopore sequencing

Ion channels are also structurally and functionally complex, requiring years of work in many cases to fully understand. But these cellular traffic regulators also have the potential to be amazing tools for scientists. The application of nanopores for DNA sequencing was highlighted in a series of talks and posters during the meeting. New approaches to fabricate nanogaps for measuring conductance across a membrane, as well as new membrane surfaces themselves, were described by researchers interested in advancing the use of these channels for fast, single-molecule sequencing. While DNA transit through the membrane remains an issue for nanopore sequencing approaches (DNA travels too quickly through the pore for conductance changes to be “read”), Ian Derrington from the University of Washington discussed his and his colleagues’ work with polymeric sequences and duplex interruptions to overcome this issue.

Imaging advances

Understanding protein folding remains an incredible challenge for biochemists. Since it is a multi-step process that occurs incredibly fast being able to see protein folding requires tricks to capture snapshots of folding moments which can then be assembled to explain how various proteins arrive at their active form. Jane Clarke from the University of Cambridge was awarded the 2010 Outstanding Investigator award in the field of singl- molecule biology from the Biophysical Society for her work using single-molecule FRET approaches to tease apart some of the ways that proteins fold. A

nother award winner, Mark Schnitzer from Stanford University who received the society’s 2010 Michael and Kate Bárány Award for Young Investigators, described his lab’s work over the past few years to develop very small two-photon microscopes that can be mounted to the head of an animal for real-time, long-term cellular imaging of human and rat tissues. Schnitzer and his colleagues have reported imaging sarcomere activity in humans in real time, and they are now working on imaging brain function in both humans and rats. Their microscope weighs only 1.1 grams.


This year’s Biophysical Society meeting also provided peeks into the future of biological research; turns out nanorobots are now on the move. Nils Walter’s group from the University of Michigan described their soon-to-be published work on designing a nanorobot that looks like a spider and can “walk” across a coated surface. The group’s spiders consist of a streptavidin body attached to 8–17 biotintylated deoxyribozyme “legs.” On an avidin coated surface, the spiders lift and drop their legs off the coated surface based on the cleavage of the zinc substrate added to the surface. Different walks can be undertaken depending on the design of the surface.

The 54th annual meeting of the Biophysical Society was held at the Moscone Center in San Francisco, Feb. 20–24, 2010. More information on the meeting can be found at the society’s web site.