Located in Markstein 101 from 12:00-1:00 PM
Leading chemistry and biochemistry researchers present their new discoveries in an hour-long seminar. These events are free to the public. Students from all disciplines are highly recommended to attend and participate.
Fluorescent nucleoside analogues are powerful tools in biophysics, but despite decades of progress, important performance limits of these probes remain. To challenge these limits, a series of structurally modified tricyclic cytidine analogues were synthesized and studied using fluorescence spectroscopy and with DNA and RNA polymerases. Patterns of electronic modification were related to the color of fluorescence emission, and a record brightest known fluorescent cytidine analogue was identified. More importantly, our studies of these compounds in duplex DNA revealed that one of the compounds, 8-DEA-tC, has the highly desirable and previously unavailable property of becoming fluorescent only upon the formation of double-stranded DNA with a perfect sequence match.
Atropisomerism, or axial chirality, is a potentially dynamic form of chirality that is ubiquitous throughout the biologically active small molecule world. We aim to harness atropisomerism as a tool modulate the properties of small molecules towards improved drugs and chemical probes. Obtaining these goals has forced us to design and discover new chemical reactions.
CSUSM Alumni who have received their BS degrees in chemistry & biochemistry are invited. They have been asked back to give advice on industrial careers and the job market. Students will have the opportunity to ask questions. The panel will also highlight job opportunities at Glanbia Nutritionals, located in Carlsbad.
Fast-folding WW domains (30-50 amino acids in length) are among the best-characterized systems for comparing experiments and simulations of protein folding. Recent microsecond-resolution experiments and long duration single-trajectory modeling have shown that mechanistic changes in folding kinetics due to mutation can now be analyzed. To benchmark predictions made by simulations, recent work will be reviewed on T-jump relexation kinetics in conjunction with protein engineering that afford mutational phi-values as indicators for folding transition state structure of side chains, backbone hydrogen bond, and various loop insertion and deletion mutants of the 34-residue human Pin1 WW domain. 45 cross-validated, non-perturbative consensus mutants could be identified that provide structural constraints for transition state structure within all WW domain substructures (core, loops, β-sheet). The robustness of two conserved hydrophobic miniclusters in the folding transition state will be probed and mutations and positions along the sequence that perturb the energy landscape and change the folding mechanism in aqueous buffer will be identified. In a cellular context, many proteins begin to fold co-translationally, when the nascent chain is still attached to the ribosome. Contrary to folding of isolated proteins in vitro, co-translational folding is vectorial and starts as soon as the protein emerges from the peptide exit tunnel of the ribosome. We’ve developed fully reconstituted in vitro translation systems which, in conjunction with biophysical techniques (e.g. FRET) and limited proteolysis, can be used to study protein translation kinetics and folding on synchronized ribosomes in real-time.
Wednesday, May 9, 2018. Science Hall 2, 1st floor patio. 3:00-4:30 PM.
Research Poster Showcase and Award Recognition.
"Frontiers in Science is a scientist speaker series exploring the new discoveries at the interface of astronomy, biology, chemistry, computer science, mathematics, physics and engineering. These seminars introduce audiences from all disciplines and academic levels to the intrigue and fun of scholarly pursuits in the natural and physical science disciplines.
March 10, 2018
"Explore interactive demonstrations and hands-on science activities at Super STEM Saturday, including rocket launches, build-a-robot stations, model displays, scientist chats and a obstacle course. The event is free and open to the public. Complimentary parking available in Lot F."