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Physics News Update
Number 803, November 29, 2006 by Phil Schewe, Ben Stein, and Davide Castelvecchi

Protein Folding in a Curved Space

Physicists at the Università di Firenze, in Italy, have put a new slant on the protein folding problem. Proteins are special polymers made of amino acids. Generic polymers, when you cool them enough, will collapse in a ball. Proteins do something more interesting: they fold up into a particular compact form. If a protein fails to find this form it won't be able to carry out its designated function and disease can result. For instance, some nonfolding proteins will aggregate into long filaments, amyloid fibrils, and this has proven to be the basis for neurodegenerative diseases like Alzheimer's.

Finding the precise dynamics behind protein folding would be like Isaac Newton finding the laws of universal gravitation. We aren't at that point yet, but there are ways of investigating some of the steps proteins take to arrive at their proper form. One fruitful approach is to see the multi-step process as taking place in a series of energy transactions. At any moment the protein can be represented as a point moving around in an abstract space whose coordinates correspond to all possible configurations and the associated energy needed to have that structure, sort of like a ball rolling along on the inner surface of a bowl. The bowl might have some partitions, and the ball might be able to roll up out of one compartment and into a neighboring one if its energy is sufficient, or if the wall between compartments is low enough, or if some extra energy (maybe in the form of heat or a chemical reaction) is added.

Lapo Casetti (casetti@fi.infn.it) and Lorenzo Mazzoni have attempted to make the "energy landscape" method even more geometrical by characterizing the folding forces at work as being a form of curvature in the bowl-like well in which the protein is operating. This is analogous to what Albert Einstein did in characterizing gravity as the curvature of spacetime in which planets and stars move about. Mazzoni and Casetti seek to determine what it is about the curvature of the energy landscape that encourages proteins to fold and other polymers not to fold.

Mazzoni and Casetti, Physical Review Letters, 24 November 2006
Contact Lapo Casetti
Università di Firenze
casetti@fi.infn.it

Warm Detectors Look At Brain Magnetism

The brain and heart both generate weak magnetic fields which, in ways different from electric fields, can reveal subtle clues about such maladies as epilepsy and arrhythmias. Sensitive magnetometers, based on superconducting quantum interference devices (SQUIDs), have been used to prepare detailed magnetoencephalograms (MEGs). Unfortunately, these devices require liquid helium and all its associated cryogenic equipment.

Michael Romalis, a Princeton University physicist, detects the brain's faint magnetic fields using instead a vessel filled with potassium atoms, which have been polarized by a laser beam. The brain fields cause the potassium atoms to precess in a measurable way. Already, Romalis (romalis@princeton.edu) says, his device has attained a sensitivity 30 times better than previous atomic magnetometers used for biosensors, and a spatial resolution comparable to that for SQUIDs, with the prospect of improving by another factor of ten.

In a related paper, Romalis's group in collaboration with Karen Sauer from George Mason University used a different kind of potassium magnetometer to detect radio-frequency signals generated by ammonium nitrate (which is often used in explosives) with a sensitivity some 10 times better than with conventional devices.

Xia et al. and Lee et al., two articles in Applied Physics Letters, 20 November 2006
More information from Romalis's Web page

Optical Beehive

A team of Italian and German physicists has developed a new, flexible fabrication technique for rewritable photonic crystal devices, which could make it easier to create and modify circuits in which photons process information in the same way that electric currents do in electronics.

Photonic crystals are structures with a periodically varying refractive index that affects the transmission of light inside the crystal; they behave like a mirror by blocking light propagation at some wavelengths and behave like a transparent medium by letting other wavelengths get through. Defects in the periodic structure, arranged in specific geometries, can act as resonant cavities, mirrors, waveguides, or the optical analogue of transistors.

The new technique is based on a two-dimensional lattice of microscopic pores arranged in a beehive pattern. The researchers can then insert defects by injecting different materials into the pores, which are a few hundreds of nanometers wide. In the photonic crystal, light is mostly confined to the two-dimensional structure, but small amounts leak outside of the plane and can be read out with a near-field microscope. Francesca Intonti, of the European Laboratory for Non-linear Spectroscopy, in Florence, says that the technique makes it easier and more flexible to experiment with different materials and configurations, compared with other fabrication techniques such as lithography; using liquids also allows for the circuits to be reconfigured at will. Another possibility, she says, could be to inject liquid crystals, whose refraction index could then be tuned from the outside, or light-emitting materials, which could act as local sources of laser light. So far, the researchers have created photonic components pixel by pixel, but in principle the process could be automatized, Intonti says.

Intonti et al., Applied Physics Letters, 20 November 2006
Contact Francesca Intonti
European Laboratory for Non-linear Spectroscopy
Tel: +39-055-4572499
intonti@lens.unifi.it
Also see: PNU 633

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