Difference between revisions of "Part:BBa K5036001"
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This is known as the tobacco etch virus which is very selective for cleaving proteins at particular amino acid sequences and has been modified to have better qualities like greater heat stability, decreased self-cleavage and also  allows researchers to precisely cleave the tag off, leaving behind the receptor in its unmodified form.
 
This is known as the tobacco etch virus which is very selective for cleaving proteins at particular amino acid sequences and has been modified to have better qualities like greater heat stability, decreased self-cleavage and also  allows researchers to precisely cleave the tag off, leaving behind the receptor in its unmodified form.
 
In our model TEV was divided into N-terminal and C-terminal fragments. So the C-terminal fragment was grafted onto dCAS9(C) to generate TEV(C)-dCas9(C).
 
In our model TEV was divided into N-terminal and C-terminal fragments. So the C-terminal fragment was grafted onto dCAS9(C) to generate TEV(C)-dCas9(C).
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==Literature Characterization==
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This study investigated five mutations introduced into the TEV protease enzyme to improve its solubility. Following the mutations, a technique involving centrifugation was used to evaluate the solubility of each variant. The variants were concentrated ,samples were collected at specific time points, and then the protein concentrations were measured to assess their solubility.
  
 
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Revision as of 15:26, 9 September 2024


C-TEV

Part Description

This is known as the tobacco etch virus which is very selective for cleaving proteins at particular amino acid sequences and has been modified to have better qualities like greater heat stability, decreased autolysis (self-cleavage) and also allows researchers to precisely cleave the tag off, leaving behind the receptor in its unmodified form. In our model, TEV was divided into N-terminal and C-terminal fragments. So the C-terminal fragment was grafted onto dCAS9(C) to generate TEV(C)-dCas9(C).

Usage

This is known as the tobacco etch virus which is very selective for cleaving proteins at particular amino acid sequences and has been modified to have better qualities like greater heat stability, decreased self-cleavage and also allows researchers to precisely cleave the tag off, leaving behind the receptor in its unmodified form. In our model TEV was divided into N-terminal and C-terminal fragments. So the C-terminal fragment was grafted onto dCAS9(C) to generate TEV(C)-dCas9(C).

Literature Characterization

This study investigated five mutations introduced into the TEV protease enzyme to improve its solubility. Following the mutations, a technique involving centrifugation was used to evaluate the solubility of each variant. The variants were concentrated ,samples were collected at specific time points, and then the protein concentrations were measured to assess their solubility.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 310