The peptides are derived from larger proteins that are active in infection, nuclear translocation and budding of new viruses. The current project, peptide MA31, is derived from the N-terminus of the Gag Matrix protein; this has been one focus of three of our trips to CHESS, the most recent in March, 2015.
Ashley is currently working for mentor Aaron Stebner, Assistant Professor in Mechanical Engineering and Materials Science at the Colorado School of Mines. She graduated with a B.S. in Mechanical Engineering from the University of Wyoming in August 2013 and is currently in her second year pursuing a Ph.D. in Mechanical Engineering with a thesis title “Quantifying the Multiscale Mechanics of Phase Transformation, Twinning, and Slip Using High Energy Diffraction Microscopy”.
Synchrotron radiation sources have enabled revolutionary applications, that are advancing understanding of the electronic and structural nature of atomic scale systems containing transition-metal atoms.
CHESS is pioneering the development of new x-ray optics and spectrometers for this purpose and a small, extremely productive community of users has grown with this capability. It is now time for a workshop focused on communicating what we have learned, building interest, and instructing a new generation of scientists on these methods.
At the lowest level, compaction is achieved by wrapping stretches of DNA around a core of histone proteins to form nucleosomes in a “beads on a string” configuration: 147 base pairs of DNA per nucleosome, with linkers of variable length between nucleosomes. The nucleosome core particle (NCP), or one “bead”, consists of 4 types of histone (H2A, H2B, H3, and H4), each of which has a compact core plus a positively-charged, flexible tail that protrudes from the core.
The paper “Dynamics and Rheology of Soft Colloidal Glasses” came out in the January 7th edition [1].
Now housed inside the Wilson Synchrotron Laboratory, the MLC is the latest addition to Cornell’s own particle accelerator located under Alumni Field.
The MLC is the product of over twenty thousand hours of work within Newman Lab, built and designed with the help of a grant from the National Science Foundation to explore technologies for use in the next generation of particle accelerators. Its seven superconducting cavities funnel energy into particle beams to help scientists study, basic building blocks of matter, solid state physics and even human biology.
Most of us have never purposely removed the innards of any computer just to see what pieces fit where, or how each complex element is intentionally connected to another. A group of students from the Greater Ithaca Activities Center are doing just that -- spending six weeks this spring removing, identifying, labeling and reassembling the hardware of old computers to learn how the major components work in synchrony as one powerful device.
However, students from the groups of Brian Korgel and Tom Truskett at the University of Texas at Austin, found just the opposite behavior in superlattices of small gold nanoparticles [1]. These consist of a 2 nm gold core surrounded by organic octodecane thiol ligands with about the same length. Upon casting from solution, these particles form superlattices with a BCC structure [2]. Similar to block copolymer micelles with sufficiently long ligands the BCC lattice is favored over the denser FCC lattice, as the entropy of the ligands is maximized [3,4].
Most commercial rechargeable batteries are based on lithium ion intercalation into layered metal oxides, the mechanism of which is fairly well understood. To move forward in the development of better electrode materials, deeper insights into heretofore unexplored methods of charge storage must be gained.
Integral membrane proteins also are notoriously hard to synthesize and study, which explains why so few have been fully, three-dimensionally characterized with protein crystallography. Using standard recombinant DNA techniques and some novel design principles, Cornell chemical engineers have developed a new method for making large quantities of integral membrane proteins simply and inexpensively – all without the use of harsh chemicals, or detergents, typically used today.