Research Highlights

The hunt was afoot within the laboratory of JILA and NIST Fellow Ralph Jimenez as his team continued to unravel the mystery of entangled two-photon absorption. Entangled photons are pairs of light particles whose quantum states are not independent of each other, so they share aspects of their properties, such as their energies and angular momenta. For many years, these photons have been studied by physicists who are trying to create quantum networks and other technologies. The Jimenez lab has been researching whether entangled photons can excite molecules with greater, even super, efficiency as compared with normal photons. 

In a new paper published in the Journal of Physical Chemistry Letters, Jimenez and his team report a new experimental setup to search for the cause of a mysterious fluorescent signal that appears to be from entangled photon excitation. According to Jimenez: “We built a setup where you could use either a classical laser or entangled photons to look for fluorescence. And the reason we built it is to ask: ‘What is it that other people were seeing when they were claiming to see entangled photon-excited fluorescence?’ We saw no signal in our previous work published a year ago, headed by Kristen Parzuchowski. So now, we're wondering, people are seeing something, what could it possibly be? That was the detective work here.” The results of their new experiments suggested that hot-band absorption (HBA) by the subject molecules, could be the potential culprit for this mysterious fluorescent signal, making it the prime suspect. 

Most researchers would agree that it is much easier to write a paper about an observed effect than a paper proving the nonexistence of the effect when it is not observed. NIST JILA Fellow Ralph Jimenez found this to be the case in contributing to a recent paper published in Physical Review Applied. The authors of this paper were originally hoping to observe the increased efficiency in two-photon absorption, a special type of process used in microscopy of living tissue, that had been reported by other research labs. This increased efficiency would be determined by an additional absorption signal than the one being produced by classical light. This additional signal came from using entangled photons. Instead, Jimenez and his team of collaborators from NIST found no additional signal in their measurements, indicating a lack of absorption entirely from the entangled photons. 

How do you find a single cell in a sea of thousands? You make it glow. Adding fluorescence helps track movement and changes in small things like cells, DNA, and bacteria. In a library of millions of cells or bacteria, flow cytometry sorts the glowing material you want to study from the non-glowing material.

The actors are molecules. The plot, broken molecular bonds. JILA Fellow Ralph Jimenez and a team of detector experts at the National Institute of Standards and Technology (NIST) are working together to make X-ray movies of a molecular drama. The team at NIST built a microcalorimeter X-ray spectrometer capable of performing time-resolved spectroscopy; in other words: a camera to film molecules. They use this camera to learn how molecules break their bonds – do the ­electrons rearrange, do the other atoms quake?

Far-red fluorescent light emitted from proteins could one day illuminate the inner workings of life. But before that happens, scientists like Fellow Ralph Jimenez must figure out how fluorescent proteins’ light-emitting structures work. As part of this effort, Jimenez wants to answer a simple question: How do we design red fluorescent proteins to emit longer-wavelength, or redder, light?

Because red fluorescent proteins are important tools for cellular imaging, the Jimenez group is working to improve them to further biophysics research. The group’s quest for a better red-fluorescent protein began with a computer simulation of a protein called mCherry that fluoresces red light after laser illumination. The simulation identified a floppy (i.e., less stable) portion of the protein “barrel” enclosing the red-light emitting compound, or chromophore. The thought was that when the barrel flopped open, it would allow oxygen in to degrade the chromophore, thus destroying its ability to fluoresce.

Graduate student Jennifer Lubbeck (Jimenez Group) spent the summer of 2011 doing research in the Molecular Spectroscopy Laboratory at the RIKEN Institute in Wako, Japan (near Tokyo). Her host's group included 16 postdocs and four graduate students. The group was under the direction of Chief Scientist Tahei Tahara. However, Lubbeck actually worked directly with just five other young scientists under the supervision of Professor Kunihiko Ishi (Ishi-san).

Fellow Ralph Jimenez is applying his knowledge of lasers, microscopy, and the precise control of tiny amounts of fluids to the development of a battery-powered blood analyzer for use "off-grid" in Third World countries. He is collaborating with Jeff Squier, David Marr, and their students from the Colorado School of Mines and Charles Eggleton and his student from the University of Maryland, Baltimore County, to see if they can come up with a fast and accurate way to measure the elasticity, or stiffness, of individual red blood cells as they flow through an "optical lab on a chip."

Fellows Steve Cundiff and Ralph Jimenez have created two precision optics instruments with a priceless potential for shedding light on condensed-matter and biological physics. Instrument shop staffer Kim Hagen aided and abetted them in their endeavor by creating exquisite CAD drawings and machining precision parts.

An excellent way to watch proteins fold is to probe the inside of a microfluidics device with light. This tiny device contains micron-sized three-dimensional (3D) transparent channels that carry small amounts of liquid. Inside the channels, the fluid flow is laminar, i.e., there is no turbulence. Consequently, fluid flow through them is predictable and easily modeled. Microfluidics devices have been used to study chemical reaction kinetics and control chemical and biological reactions.

Fellows Ralph Jimenez and Henry Kapteyn and their groups recently helped develop optical technology that will make femtosecond laser experiments much simpler to perform, opening the door to using such lasers in many more laboratories. The technology, which employs reflection grisms as laser pulse compressors, has been patented and is now available commercially. A reflection grism consists of metal reflection grating mounted on one face of a prism.

Our lives depend on heme. As part of hemoglobin, it carries oxygen to our tissues. As part of cytochrome c, it helps transform the energy in food into the energy-rich molecule ATP (adenosine triphosphate) that powers biochemical reactions that keep us alive and moving. As part of cytochrome P450, it helps break down toxic chemicals in our bodies.