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|
| Type |
Symposium |
| Area |
Frontiers in Chemical Biology & Protein Chemistry |
| Room No. |
Room C311+C312 |
| Time |
FRI 09:00-: |
| Code |
BIO-1 |
| Subject |
Engineered protein assemblies to utilize biomolecular multivalency |
| Authors |
Yongwon Jung
Department of Chemistry, Korea Advanced Institute of Science and Technology, Korea |
| Abstract |
Multivalency is a key principle in nature for many biological processes such as cell-cell communications, phase separation, and even simple DNA hybridization. For example, multivalent interactions between cells or with other organisms (bacteria and viruses) are governed by multiple ligand-receptor interactions on cell surfaces. Simple (and often weak) individual biomolecular interactions can be highly strengthened and diversified by employing multivalency. To study and employ multivalent bio-interactions, however, multivalent scaffold architectures that can display multivalent biomolecules in a well-defined manner must be developed. Here I will introduce several new strategies to fabricate large protein assemblies, which can be valuable assets to utilize multivalent protein interactions. In particular, modifications and applications of fluorescent proteins, avidin proteins, and cage proteins with highly interesting binding properties will be discussed. Several examples of how newly fabricated protein assemblies can be applied in bioanalytical or biomedical applications will also be discussed. |
| E-mail |
ywjung@kaist.ac.kr |
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120th General Meeting of the KCS