Biosciences News

“Our approach provides new evidence of a limited but unequivocal plasticity of the genetic code whose secrets still lie hidden in the majority of unsequenced organisms.”

Published ahead online March 16, 2016 in the journal Angewandte Chemie International Ed., researchers from the DOE Joint Genome Institute and Yale University have discovered that microorganisms recognize more than one codon for the rare, genetically encoded amino acid selenocysteine. The finding adds credence to recent studies indicating that an organism’s genetic vocabulary is not as constrained as had been long held. Read more about this study on the DOE JGI website.

To see biochemist Ee-Been Goh in the lab today, figuring out how to rewire bacteria to produce biofuels, one would never guess she was once so uninterested in school that she barely made it through junior high. Today she is a project scientist at the Joint BioEnergy Institute (JBEI), a Department of Energy Bioenergy Research Center led by Lawrence Berkeley National Laboratory. Read more at Berkeley Lab News Center.

Berkeley Lab researchers have discovered a family of nature-inspired polymers that, when placed in water, spontaneously assemble into hollow crystalline nanotubes. These nanotubes can be tuned to all have the same diameter of between five and ten nanometers, depending on the length of the polymer chain. Ken Downing, biophysicist senior scientist in the Molecular Biophysics & Integrated Bioimaging Division, was part of the team that worked to develop and characterize the nanotubes, which have many potential uses, such as delivering cancer-fighting drugs inside cells or desalinating seawater. Read more at Berkeley Lab News Center.

Currently in its ninth year of operation, JBEI has made remarkable scientific progress toward the development of renewable bioenergy solutions. Fundamental to JBEI’s mission is also its commitment to preparing the next generation of scientists, promoting the benefits of biofuels and expanding broad interest in science. In light of this commitment, JBEI has debuted nine short videos in a series entitled “Bioenergy Research @ JBEI”. To watch the videos visit JBEI’s YouTube channel.

Naturally occurring proteins—chains of amino acids that fold into functional, three-dimensional shapes—are believed to represent just a small fraction of the universe of all possible permutations of amino-acid sequences and folds. How can we begin to systematically sift through those permutations to find and engineer from scratch (de novo) proteins with the characteristics desired for medical, environmental, and industrial purposes? To address this question, a team led by researchers from the Institute for Protein Design at the University of Washington have published a landmark study that used both protein crystallography (Beamlines 8.2.1 in the Berkeley Center for Structural Biology and 8.3.1) and small-angle x-ray scattering (SAXS; SIBYLS Beamline) at the ALS to validate the computationally designed structures of novel proteins with repeated motifs. The results show that the protein-folding universe is far larger than realized, opening up a wide array of new possibilities for biomolecular engineering. Read the ALS Science Highlight.