User:Jeff Quinn: Difference between revisions

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*By inserting the sequence of one protein into the sequence of another, the functionality of the protein can be lost; however, the new chimeric protein can assume new characteristics.  For example, by inserting the sequence for an allosteric substrate-binding protein into the sequence of a metabolic enzyme, it is possible that the two proteins together can behave in a new way: as a switch.  When substrate binds to the chimera, it can induce a conformational change in the enzyme that either activates or inactivates its enzymatic behavior, effectively creating a novel control mechanism for modulating the enzyme's activity with an input molecule (the substrate).
*By inserting the sequence of one protein into the sequence of another, the functionality of the protein can be lost; however, the new chimeric protein can assume new characteristics.  For example, by inserting the sequence for an allosteric substrate-binding protein into the sequence of a metabolic enzyme, it is possible that the two proteins together can behave in a new way: as a switch.  When substrate binds to the chimera, it can induce a conformational change in the enzyme that either activates or inactivates its enzymatic behavior, effectively creating a novel control mechanism for modulating the enzyme's activity with an input molecule (the substrate).
*Based on the experiment described by Guntas and Ostermeier, we plan to develop our own "molecular switch" protein in the same way that they did, by creating an allosteric enzyme that "couples effector levels (input) to enzyme activity (output)."   
*Based on the experiment described by Guntas and Ostermeier, we plan to develop our own "molecular switch" protein in the same way that they did, by creating an allosteric enzyme that "couples effector levels (input) to enzyme activity (output)."   
*Proteins to work with (IDEAS):
*Enzymes to work with (IDEAS):
**hemoglobin
**hemoglobin
**EGFP
**EGFP
**pyruvate decarboxylase
**
*Substrate-Binding proteins to work with (IDEAS):
**calmodulin
**


===Background Information===
===Background Information===

Revision as of 14:23, 28 April 2008

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Contact Info

Jeff Quinn

Jeffrey Quinn, MIT 2010, Course 20

  • (916)765-9607
  • jquinn[at]mit.edu

Module 3 Research Proposition Information

Project Overview

  • By inserting the sequence of one protein into the sequence of another, the functionality of the protein can be lost; however, the new chimeric protein can assume new characteristics. For example, by inserting the sequence for an allosteric substrate-binding protein into the sequence of a metabolic enzyme, it is possible that the two proteins together can behave in a new way: as a switch. When substrate binds to the chimera, it can induce a conformational change in the enzyme that either activates or inactivates its enzymatic behavior, effectively creating a novel control mechanism for modulating the enzyme's activity with an input molecule (the substrate).
  • Based on the experiment described by Guntas and Ostermeier, we plan to develop our own "molecular switch" protein in the same way that they did, by creating an allosteric enzyme that "couples effector levels (input) to enzyme activity (output)."
  • Enzymes to work with (IDEAS):
    • hemoglobin
    • EGFP
    • pyruvate decarboxylase
  • Substrate-Binding proteins to work with (IDEAS):
    • calmodulin

Background Information

Research Problem and Goals

Methods

Projected Results

Resources