Difference between revisions of "Louis Badang Chem430 F16"
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==Research Times== | ==Research Times== | ||
| − | T/Thur 2 | + | T/Thur 10:00am - 2:00pm |
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: section 02 = 0.50 credit = 8 hours per week. | : section 02 = 0.50 credit = 8 hours per week. | ||
==Proposed Research Project== | ==Proposed Research Project== | ||
===Enter Project Title here=== | ===Enter Project Title here=== | ||
| − | The Effect of the Removal of a Salt Bridge on the Activity of the FNR Transcription Factor | + | The Effect of the Removal of a Salt Bridge on the Activity of the FNR Transcription Factor (The Second Part) |
===General Information=== | ===General Information=== | ||
:Advisor: Laura Moore | :Advisor: Laura Moore | ||
:Other research student collaborators: Sobhi Kazmouz | :Other research student collaborators: Sobhi Kazmouz | ||
| − | |||
===Proposal=== | ===Proposal=== | ||
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===Instruments to be used=== | ===Instruments to be used=== | ||
| + | UV/Vis spectrophotometry | ||
===References (2 minimum)=== | ===References (2 minimum)=== | ||
Latest revision as of 00:41, 1 October 2016
Chemistry/Biochemistry Research 430
- Fall 2016
- Styles Bitchly
- Junior Biochemistry Major
Research Times
T/Thur 10:00am - 2:00pm
- section 02 = 0.50 credit = 8 hours per week.
Proposed Research Project
Enter Project Title here
The Effect of the Removal of a Salt Bridge on the Activity of the FNR Transcription Factor (The Second Part)
General Information
- Advisor: Laura Moore
- Other research student collaborators: Sobhi Kazmouz
Proposal
The salt bridge interaction between Asp 130 and Arg 140 is essential for the dimerization of FNR. In this research, I will produce a double mutant FNR where Asp 130 will be changed into Arg and Arg 140 into Glu at the same time. This is to show definitely that the salt bridge is important to the FNR to dimerize in the absence of oxygen. Also, another mutation that may be done is Arg to Asp 140 mutation to check whether the lack of compatibility in activity values of both mutant FNR samples is caused by the distinction between the size of the R group of the aspartate and glutamate residue.
Instruments to be used
UV/Vis spectrophotometry
References (2 minimum)
Moore, L. J., & Kiley, P. J. (2001). Characterization of the Dimerization Domain in the FNR Transcription Factor. Journal of Biological Chemistry, 276(49), 45744-45750. doi:10.1074/jbc.m106569200
Volbeda, A., Darnault, C., Renoux, O., Nicolet, Y., & Fontecilla-Camps, J. C. (2015). The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium. Science Advances, 1(11). doi:10.1126/sciadv.1501086
Research pledge
I, Louis J Badang, have read the Chem/Bioc 430 course syllabus and understand the general structure and expectations of the research program. The above material was prepared after consultation, and in conjunction with my research advisor.