Welcome to the Quiroz Lab!
The Quiroz Lab mines protein self-assembly across engineered and biological systems. Led by Felipe Garcia Quiroz, we are a diverse team of scientists and biomolecular engineers.
Members of the Quiroz Lab engineer self-assembling materials that are genetically-encoded and stimuli-responsive. Using these materials, together with genetic and protein engineering tools, we tackle exciting challenges in nanotechnology, biotechnology and medicine. We are also interested in dissecting the DNA and genomic parts that encode for such material systems and their emergent biophysical properties at the DNA/genome and protein levels. To learn new principles of self-assembly and stimuli-responsiveness, we take a bioinspired approach. We probe and manipulate self-assembly phenomena within cells and tissues. The resulting findings illuminate fundamental aspects of biology and serve as foundation to engineer advanced biomaterials.
We are part of the Wallace H. Coulter Department of Biomedical Engineering at Georgia Tech and Emory University. Check out our website for more details on our research directions, publications and funding.
[April 12, 2021] Our research informs new avenues to engineer synthetic cells.
[March 20, 2021] The Italy-based International Center for Theoretical Physics just uploaded a recent research talk from our group.
[March 3, 2021] Why join Coulter BME? Here from us, students and faculty at GT/Emory.[October 7, 2020] We welcome Kai Littlejohn and Camila Giraldo as new PhD students. [August 3, 2020] We welcome Alexa Avecilla, who just joined the lab as a PhD student. [March 13, 2020] Our most recent work on liquid-liquid phase separation in skin was just published in Science!
ABOUT THE COVER ART
The art in our homepage was created by Markos Kay for the Quiroz Lab. This illustration depicts our efforts to engineer and dissect the self-assembly of genetically-encoded materials. In nature, these complex materials are often built from simple, repetitive and disordered building blocks. Here, intrinsically-disordered proteins, at the bottom, assemble over space and time to yield highly-ordered nanostructures on the surface.