Abstract Title
Titin
Additional Funding Sources
The work presented here was supposed by Institutional Development Awards (IDeA) from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under the following Grant Nos. Idaho INBRE: P20GM103408, Montana INBRE: P20GM103474. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
Abstract
Nucleophosmin (NPM1) interacts with other scaffolding proteins to bring together two or more proteins in a relatively stable configuration. This is done to maintain the liquid-like matrix of the nucleolus. It has been seen that titin has multiple structural elements that are similar in their characteristics to NPM1. Overall, we suspect that titin binds NPM1, in order to test, we will work to purify NPM1 and titin over the summer in order to test the potential binding domains of NMP1 within titin. This will be done by using surface plasmon resonance to screen the binding domains to NPM1. In addition, mass spectrometry is used to test the possible interaction between NPM1 and titin.
Titin
Nucleophosmin (NPM1) interacts with other scaffolding proteins to bring together two or more proteins in a relatively stable configuration. This is done to maintain the liquid-like matrix of the nucleolus. It has been seen that titin has multiple structural elements that are similar in their characteristics to NPM1. Overall, we suspect that titin binds NPM1, in order to test, we will work to purify NPM1 and titin over the summer in order to test the potential binding domains of NMP1 within titin. This will be done by using surface plasmon resonance to screen the binding domains to NPM1. In addition, mass spectrometry is used to test the possible interaction between NPM1 and titin.