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| Type |
Award Lecture in Division |
| Area |
Mass Spectrometry in Chemical Biology |
| Room No. |
Room 407+408 |
| Time |
FRI 09:00-09:30 |
| Code |
LIFE2-1 |
| Subject |
Investigation of Dynamic Features of Proteins Using NMR Spectroscopy |
| Authors |
Yangmee Kim
Department of Bioscience and Biotechnology, Konkuk University, Korea |
| Abstract |
Flexibilities in protein conformations are essential for their functions. The relationship between protein structure, dynamics, and function is very challenging to study because the conformational space available to a protein is extensive and the time scales of conformational motions range widely, from picoseconds to seconds. These time scales are accessible by solution NMR making it a suitable technique for investigating the motions in proteins. Loop regions connecting secondary structural elements are highly dynamic and their motions play important roles in protein function. For example, the flexibility of the WPD loop as well as P-loop of phosphatase is closely related to its catalytic activity. Relaxation dispersion measurements can provide the closing rate of loops in phosphatases which play a role in the substrate recognition. The flexible recognition loops in acyl carrier protein (ACP) play key roles in communication with proteins in fatty acid synthase (FAS). We investigated these interactions between ACP and bacterial FAS proteins, which can be good targets for development of antibiotics. Also, the surface loop flexibility of cold shock protein is important to accommodate nucleic acids upon cold shock. The importance of dynamic features of proteins for their molecular recognition processes and their catalytic activities will be demonstrated using spin relaxation approaches, showing that solution NMR spectroscopy is a strong tool for study of protein dynamics and functional consequences. |
| E-mail |
ymkim@konkuk.ac.kr |
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123rd General Meeting of the KCS