Justas2010 (Talk | contribs) |
Justas2010 (Talk | contribs) |
||
Line 51: | Line 51: | ||
<p>Aistė Skrebytė was the person at the Vilnius University Rector’s office that we could rely on. She helped our team with financial questions - team’s registration, Giant Jamboree-fee payments, and many others. She was always there for our team and tried to find best solutions to our organizational difficulties including our trip to Boston and general PR strategy.</p> | <p>Aistė Skrebytė was the person at the Vilnius University Rector’s office that we could rely on. She helped our team with financial questions - team’s registration, Giant Jamboree-fee payments, and many others. She was always there for our team and tried to find best solutions to our organizational difficulties including our trip to Boston and general PR strategy.</p> | ||
+ | |||
+ | <h1>Additional Thanks</h1> | ||
+ | |||
+ | |||
+ | <strong>Audrius Žemys</strong> | ||
Revision as of 19:33, 16 October 2018
Attributions
Lorem ipsum, dolor sit amet consectetur adipisicing
Cell-free systems are becoming an increasingly popular in vitro tool to study biological processes as it is accompanied by less intrinsic and extrinsic noise. Relying on fundamental concepts of synthetic biology, we apply a bottom-up forward engineering approach to create a novel cell-free system for unorthodox protein-evolution. The core of this system is cell-sized liposomes that serve as excellent artificial membrane models. By encapsulating genetic material and full in vitro protein transcription and translation systems within the liposomes, we create reliable and incredibly efficient nanofactories for the production of target proteins. Even though there are many alternative proteins that can be synthesized, our main focus is directed towards membrane proteins, which occupy approximately one third of living-cells’ genomes. Considering their significance, membrane proteins are spectacularly understudied since synthesis and thus characterization of them remain prevailing obstacles to this day. We aim to utilize liposomes as nanofactories for directed evolution of membrane proteins. Furthermore, by means of directed membrane protein-evolution, a universal exposition system will be designed in order to display any protein of interest on the surface of the liposome. This way, a system is built where a phenotype of a particular protein is expressed on the outside while containing its genotype within the liposome. To prove the concept, small antibody fragments will be displayed to create a single-chain variable fragment (scFv) library for rapid screening of any designated target.