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Team:CU-Boulder/Project/Kit/Purification
From 2013.igem.org
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| - | <dt>ELPs - Elastin-like proteins</dt> | + | <dt>ELPs - Elastin-like proteins<br></dt> |
<dd>Elastin-like proteins are simply oligomeric repeats of Val-Pro-Gly-Xaa-Gly (Xaa being any amino acid with the exception of proline). ELPs undergo reversible, inverse phase transitions at at a transition temperature or after the addition of NaCl. Below this temperature/concentration of NaCl, ELPs are soluble. So here at CU-Boulder, we are trying to take advantage of this simple, yet interesting trait of these proteins by attempting to attach these ELPs to proteins in an attempt to come up with an easy and affordable method of protein purification. This method has been proven to work in previous experiments, so we're trying to develop a iGEM part that will include an optimized ELP that will make protein purification a simple process.</dd> | <dd>Elastin-like proteins are simply oligomeric repeats of Val-Pro-Gly-Xaa-Gly (Xaa being any amino acid with the exception of proline). ELPs undergo reversible, inverse phase transitions at at a transition temperature or after the addition of NaCl. Below this temperature/concentration of NaCl, ELPs are soluble. So here at CU-Boulder, we are trying to take advantage of this simple, yet interesting trait of these proteins by attempting to attach these ELPs to proteins in an attempt to come up with an easy and affordable method of protein purification. This method has been proven to work in previous experiments, so we're trying to develop a iGEM part that will include an optimized ELP that will make protein purification a simple process.</dd> | ||
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Revision as of 20:14, 21 August 2013
- ELPs - Elastin-like proteins
- Elastin-like proteins are simply oligomeric repeats of Val-Pro-Gly-Xaa-Gly (Xaa being any amino acid with the exception of proline). ELPs undergo reversible, inverse phase transitions at at a transition temperature or after the addition of NaCl. Below this temperature/concentration of NaCl, ELPs are soluble. So here at CU-Boulder, we are trying to take advantage of this simple, yet interesting trait of these proteins by attempting to attach these ELPs to proteins in an attempt to come up with an easy and affordable method of protein purification. This method has been proven to work in previous experiments, so we're trying to develop a iGEM part that will include an optimized ELP that will make protein purification a simple process.
