Louis Badang Chem430 F16

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

Other Research Collaborators:

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.