Difference between revisions of "Part:BBa K3121003"
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We identified the Cpn 10/60 chaperone system (isolated from Oleispira antarctica). The chaperonin 10/60 is homologous to the GroEL/ES chaperonin system in E. coli. Essentially, these are active assistants for protein folding processes. The advantage here is that Cpn 10/60 is a cold-active component, i.e., unlike the mesophilic chaperone systems which are highly inefficient at lower temperatures, these cold-active entities perform optimally at cold temperatures. The Cpn 10/60 which predominantly retains a double ring form at mesophilic temperature ranges (excess of 24℃), shifts to a single ring form at lower temperatures (4-10℃). This is especially relevant since single ring conformations are more energetically efficient. | We identified the Cpn 10/60 chaperone system (isolated from Oleispira antarctica). The chaperonin 10/60 is homologous to the GroEL/ES chaperonin system in E. coli. Essentially, these are active assistants for protein folding processes. The advantage here is that Cpn 10/60 is a cold-active component, i.e., unlike the mesophilic chaperone systems which are highly inefficient at lower temperatures, these cold-active entities perform optimally at cold temperatures. The Cpn 10/60 which predominantly retains a double ring form at mesophilic temperature ranges (excess of 24℃), shifts to a single ring form at lower temperatures (4-10℃). This is especially relevant since single ring conformations are more energetically efficient. | ||
| + | https://static.igem.org/mediawiki/parts/1/19/T--IISERB_Bhopal--Cpn_10%2B60_lowppx.png | ||
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Revision as of 16:49, 21 October 2019
RBS_Cpn10+RBS_Cpn60
We identified the Cpn 10/60 chaperone system (isolated from Oleispira antarctica). The chaperonin 10/60 is homologous to the GroEL/ES chaperonin system in E. coli. Essentially, these are active assistants for protein folding processes. The advantage here is that Cpn 10/60 is a cold-active component, i.e., unlike the mesophilic chaperone systems which are highly inefficient at lower temperatures, these cold-active entities perform optimally at cold temperatures. The Cpn 10/60 which predominantly retains a double ring form at mesophilic temperature ranges (excess of 24℃), shifts to a single ring form at lower temperatures (4-10℃). This is especially relevant since single ring conformations are more energetically efficient.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1211
Illegal BamHI site found at 1277 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 70