The worlds most accurate "ruler" made with extreme ultraviolet light has been built and demonstrated with ultrafast laser pulses by scientists at JILA, a joint institute of the National Institute of Standards and Technology (NIST) and the University of Colorado at Boulder.
The new JILA ultraviolet "ruler" is made by exposing xenon gas atoms to a special type of infrared laser light called a femtosecond frequency "comb."
The new device, which consistently generates pulses of light lasting just femtoseconds (quadrillionths of a second, or millionths of a billionth of a second) in the ultraviolet region of the electromagnetic spectrum, will be described in the May 20 issue of Physical Review Letters.*
The device is expected to become an important tool for ultraprecise measurements in many fields of science, including chemistry, physics and astronomy. A ruler made with shorter wavelengths of light makes it possible to "see" more precise differences than ever before in the energy levels of light emissions that identify specific atoms, in the timing of chemical reactions, or, if additional applications are developed, in the dimensions of certain nanometer-scale objects. The new device also can be compared to a camera with ultrafast shutter speeds and consistent shot-to-shot frame speed and stability, allowing scientists to take real-time "pictures" of finer structures and dynamics. By combining many such pictures at a high speed, scientists can gain a more detailed understanding of many phenomena.
Laura Ost | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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