MBIB News

The Vilcek Foundation is honoring Ahmet Yildiz, faculty scientist in Molecular Biophysics and Integrated Bioimaging, who has demonstrated evidence of creative promise with his scientific work in the United States. Yildiz uses single molecule imaging to uncover the mechanism of molecular motors that function in living cells. As a winner of the Vilcek Prize for Creative Promise in Biomedical Science, Yildiz will receive a $50,000 cash award.

“The Vilcek Prizes for Creative Promise were established in 2009 as a complement to the Vilcek Prizes, to encourage and support young immigrants who have already demonstrated exceptional achievements, and who often face significant challenges early in their careers,” the Foundation’s website reads.

Yildiz’s story, including his unexpected journey from his native Turkey to the United States, his introduction to the American research culture, and his work across disciplines (critical in creating environments where scientific breakthroughs could more easily occur, he says), are highlighted in this ASCB member news post by Mary Spiro. The award was also announced in Physics@Berkeley.

The projects of 13 Biosciences Area scientists and engineers received funding through the FY17 Laboratory Directed Research and Development (LDRD) program. The funded projects cover a broad range of topics including the study of microbiomes in relation to their environment, plants, and gut health; catalysis for solar conversion to energy; and genomic expression in tissue. Among them were three projects related to Lab-wide initiatives. Together, these efforts account for 17.5% of the $25.2 million allocated. Lab-wide, a total of 88 projects were selected from a field of 166 proposals.

New images of structural fibers inside a cell appear in a study featured on the cover of the Journal of Cell Science special issue on 3D Cell Biology, published this month. The images, obtained by scientists in the Biosciences Area, show thread-like cytofilaments reaching into and traversing a human breast cell’s chromatin-packed nucleus. It provides the first visual evidence of a physical link by which genes can receive mechanical cues from its microenvironment.

The work leading up to the images began in the early 1980s when Biological Systems & Engineering’s Mina Bissell proposed the idea that gene expression and cell fate were dependent on their physical surroundings called extracellular matrix. The images were captured by Manfred Auer, staff scientist, and Ke Xu, faculty scientist, both in the Molecular Biophysics & Integrated Bioimaging Division. Read more at the Berkeley Lab News Center.

University of Washington (UW) researchers have designed a novel protein with properties that could lead to the generation of new photoactive proteins. This three-fold symmetric, self-assembling protein homotrimer contains a highly stable noncanonical amino acid. Noncanonical amino acids are not found among the 20 encoded amino acids in the body and can contain modifications to allow for new functionality. In this case, this amino acid contains a bipyridine group that chelates metal, thereby introducing new photochemical properties into the protein interface, and nucleating the formation of the homotrimer.

An article published last month in PNAS describes this work from a team of scientists led by David Baker at UW, which included Jose Henrique Pereira, Banumathi Sankaran, and Peter Zwart of the Molecular Biophysics & Integrated Bioimaging Division (MBIB). The MBIB scientists developed the crystal screen that was used to crystallize the novel protein and performed X-ray crystallography on Beamline 8.2.1 in the Berkeley Center for Structural Biology at the Advanced Light Source. Their X-ray crystallographic analysis of the homotrimer showed that the design process had near-atomic-level accuracy, demonstrating that computational protein design together with the utilization of noncanonical amino acids could be used to generate novel protein functions. These methods could be used to develop new therapeutics, biomaterials, and metalloproteins with useful optical or photochemical properties.

Calcium channel blockers are widely prescribed for heart and blood-vessel diseases. With the help of the high-intensity x-ray beams and remotely controlled robots at the Advanced Light Source (ALS), two groups of scientists from University of Washington have revealed, at atomic resolution, how two different classes of calcium channel blocker drugs produce their therapeutic effects. The researchers took advantage of the remotely controllable robot automounter available in the Berkeley Center for Structural Biology at the ALS to screen a large number of crystals for the best diffraction. The tunable x-ray source also allowed them to collect anomalous diffraction data at Beamlines 8.2.1 and 8.2.2 with bromine-incorporated drugs, which was critical for locating the drug molecules in the crystal. The results pave the way for optimizing these classic compounds for safer and more reliable pharmaceutical applications. Read the ALS Science Highlight.