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The purpose of this study is to know whether the primary motor cortex (M1) plays a role in the sensorimotor memory. It was hypothesized that temporary disruption of the M1 following the learning to minimize a tilt using a ‘L’ shaped object would negatively affect the retention of sensorimotor memory and thus reduce interference between the memory acquired in one context and the visual cues to perform the same task in a different context.
Significant findings were shown in blocks 1, 2, and 4. In block 3, subjects displayed insignificant amount of learning. However, it cannot be concluded that there is full interference in block 3. Therefore, looked into 3 effects in statistical analysis: the main effects of the blocks, the main effects of the trials, and the effects of the blocks and trials combined. From the block effects, there is a p-value of 0.001, and from the trial effects, the p-value is less than 0.001. Both of these effects indicate that there is learning occurring. However, when looking at the blocks * trials effects, we see a p-value of 0.002 < 0.05 indicating significant interaction between sensorimotor memories. Based on the results that were found, there is a presence of interference in all the blocks but not enough to justify the use of TMS in order to reduce interference because there is a partial reduction of interference from the control experiment. It is evident that the time delay might be the issue between context switches. By reducing the time delay between block 2 and 3 from 10 minutes to 5 minutes, I will hope to see significant learning to occur from the first trial to the second trial.
The membrane proximal region (MPR, residues 649–683) and transmembrane domain (TMD, residues 684–705) of the gp41 subunit of HIV-1’s envelope protein are highly conserved and are important in viral mucosal transmission, virus attachment and membrane fusion with target cells. Several structures of the trimeric membrane proximal external region (residues 662–683) of MPR have been reported at the atomic level; however, the atomic structure of the TMD still remains unknown. To elucidate the structure of both MPR and TMD, we expressed the region spanning both domains, MPR-TM (residues 649–705), in Escherichia coli as a fusion protein with maltose binding protein (MBP). MPR-TM was initially fused to the C-terminus of MBP via a 42 aa-long linker containing a TEV protease recognition site (MBP-linker-MPR-TM).
Biophysical characterization indicated that the purified MBP-linker-MPR-TM protein was a monodisperse and stable candidate for crystallization. However, crystals of the MBP-linker-MPR-TM protein could not be obtained in extensive crystallization screens. It is possible that the 42 residue-long linker between MBP and MPR-TM was interfering with crystal formation. To test this hypothesis, the 42 residue-long linker was replaced with three alanine residues. The fusion protein, MBP-AAA-MPR-TM, was similarly purified and characterized. Significantly, both the MBP-linker-MPR-TM and MBP-AAA-MPR-TM proteins strongly interacted with broadly neutralizing monoclonal antibodies 2F5 and 4E10. With epitopes accessible to the broadly neutralizing antibodies, these MBP/MPR-TM recombinant proteins may be in immunologically relevant conformations that mimic a pre-hairpin intermediate of gp41.