At a later stage, 3-nucleotide RNA sequences are translated into protein according to the genetic code.

The work was done at CHESS and APS by JIANQIU GUO ,YU YANG, BALAJI RAGHOTHAMACHAR, MICHAEL DUDLEY from SUNY Stony Brook and by CHESS Staff Scientist STAN STOUPIN (before he moved to CHESS).

Bunches of particles circulate around the Cornell Electron Storage Ring (CESR) at nearly the speed of light. Each one centimeter-long bunch consists of some billions of particles. In a blink of an eye the bunch of particles has traveled around the 768m circumference ring nearly 1,000,000 times.

The particles in the bunch emit photons as they speed around the ring. The photon emission heats up the particles in the bunch, where the hot particles expand and spread out. An otherwise bright beam is made dimmer, compromising its effectiveness as a tool for research.

These nanoparticles can find immediate applications in active and living systems for various purposes, such as self-propelled activity, environmental sensor, drug delivery and so on. Unlike chemistry-based techniques which take hours, this newly launched mechanical fabrication approach takes only several minutes at current stage. This breakthrough result has been reported at the early on-line release on 8 June 2017 at the Journal of the American Chemical Society [1].

Louisa Smieska and Ruth Mullett studied manuscript pages from Cornell University Library’s Division of Rare and Manuscript Collections (RMC), dating from the 13th to the 16th centuries, using X-ray fluorescence (XRF) and spectral imaging analysis.

“Our initial goal was to learn more about Cornell’s fragments and about trends in pigment use,” said Mullett, a medieval studies doctoral student. “An initial survey using a portable point XRF [p-XRF] instrument uncovered several things we weren’t expecting.”

Integral membrane proteins, or IMPs, are a major class of proteins that play crucial roles in many cellular processes, including the catalysis of disulfide bonds, which are essential for the function and stability of many proteins such as antibodies, which have significant therapeutic potential.

But IMPs are intrinsically hydrophobic and thus have low solubility in watery environments. Their natural environment is within the lipid bilayer membrane of a cell, which makes it difficult to study their structure and function.