Tunable Near-Field Radiative Heat Transfer Exceeding Blackbody Limit with Vanadium Dioxide Thin Film
This paper investigates near-field thermal radiation as the primary source of heat transfer between two parallel surfaces. This radiation takes place extremely close to the heated surfaces in study so the experimental set-up to be used will be done at the nanometer scale. The primary theory being investigated is that near-field radiation generates greater heat flux that conventional radiation governed by Planck’s law with maximum for blackbodies. Working with a phase shift material such as VO2 enables a switch-like effect to occur where the total amount of heat flux fluctuates as VO2 transitions from a metal to an insulator. In this paper, the theoretical heat flux and near-field radiation effect are modeled for a set-up of VO2 and SiO2 layers separated by different vacuum gaps. In addition, a physical experimental set-up is validated for future near-field radiation experiments.
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.