Difference between revisions of "Part:BBa K4759072:Design"
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===Design Notes=== | ===Design Notes=== | ||
| − | Through previous experimental results, we selected ferredoxin reductase PetH (SEQ ID NO.7) and ferredoxin PetF (SEQ ID NO.8) from the algae (Synechocystis PCC 6803) as the redox chaperones of OleP. The modeling group docked the two proteins, PetF and OleP, to obtain the hot spot residues and the corresponding mutated amino acids, and the petF genes were mutated by PCR to obtain the corresponding mutants. | + | Through previous experimental results, we selected ferredoxin reductase PetH (SEQ ID NO.7) and ferredoxin PetF (SEQ ID NO.8) from the algae (Synechocystis PCC 6803) as the redox chaperones of OleP. The modeling group docked the two proteins, PetF and OleP, to obtain the hot spot residues and the corresponding mutated amino acids, and the petF genes were mutated by PCR to obtain the corresponding mutants.<br> |
| + | Aspartic acid at site 67 of the PetF is mutated to tyrosine.<br> | ||
Revision as of 15:01, 12 October 2023
Design Notes
Through previous experimental results, we selected ferredoxin reductase PetH (SEQ ID NO.7) and ferredoxin PetF (SEQ ID NO.8) from the algae (Synechocystis PCC 6803) as the redox chaperones of OleP. The modeling group docked the two proteins, PetF and OleP, to obtain the hot spot residues and the corresponding mutated amino acids, and the petF genes were mutated by PCR to obtain the corresponding mutants.
Aspartic acid at site 67 of the PetF is mutated to tyrosine.
Source
ferredoxin reductase PetH (SEQ ID NO.7) and ferredoxin PetF (SEQ ID NO.8) from the algae (Synechocystis PCC 6803)