ASU Regents' Professors Open Access Works
The title “Regents’ Professor” is the highest faculty honor awarded at Arizona State University. It is conferred on ASU faculty who have made pioneering contributions in their areas of expertise, who have achieved a sustained level of distinction, and who enjoy national and international recognition for these accomplishments. This collection contains primarily open access works by ASU Regents' Professors.
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- Creators: Department of Chemistry and Biochemistry
- Creators: Buman, Matthew
Cell-sediment separation methods can potentially enable determination of the elemental composition of microbial communities by removing the sediment elemental contribution from bulk samples. We demonstrate that a separation method can be applied to determine the composition of prokaryotic cells. The method uses chemical and physical means to extract cells from benthic sediments and mats. Recovery yields were between 5% and 40%, as determined from cell counts. The method conserves cellular element contents to within 30% or better, as assessed by comparing C, N, P, Mg, Al, Ca, Ti, Mn, Fe, Ni, Cu, Zn, and Mo contents in Escherichia coli. Contamination by C, N, and P from chemicals used during the procedure was negligible. Na and K were not conserved, being likely exchanged through the cell membrane as cations during separation. V, Cr, and Co abundances could not be determined due to large (>100%) measurement uncertainties. We applied this method to measure elemental contents in extremophilic communities of Yellowstone National Park hot springs. The method was generally successful at separating cells from sediment, but does not discriminate between cells and detrital biological or noncellular material of similar density. This resulted in Al, Ti, Mn, and Fe contamination, which can be tracked using proxies such as metal:Al ratios. With these caveats, we present the first measurements, to our knowledge, of the elemental abundances of a chemosynthetic community. The communities have C:N ratios typical of aquatic microorganisms, are low in P, and their metal abundances vary between hot springs by orders of magnitude.
The aim of this study was to investigate the potential associations of reallocating 30 minutes sedentary time in long bouts (>60 min) to sedentary time in non-bouts, light intensity physical activity (LPA) and moderate- to vigorous physical activity (MVPA) with cardiometabolic risk factors in a population diagnosed with prediabetes or type 2 diabetes.
Methods
Participants diagnosed with prediabetes and type 2 diabetes (n = 124, 50% men, mean [SD] age = 63.8 [7.5] years) were recruited to the physical activity intervention Sophia Step Study. For this study baseline data was used with a cross-sectional design. Time spent in sedentary behaviors in bouts (>60 min) and non-bouts (accrued in <60 min bouts) and physical activity was measured using the ActiGraph GT1M. Associations of reallocating bouted sedentary time to non-bouted sedentary time, LPA and MVPA with cardiometabolic risk factors were examined using an isotemporal substitution framework with linear regression models.
Results
Reallocating 30 minutes sedentary time in bouts to MVPA was associated with lower waist circumference (b = -4.30 95% CI:-7.23, -1.38 cm), lower BMI (b = -1.46 95% CI:-2.60, -0.33 kg/m2) and higher HDL cholesterol levels (b = 0.11 95% CI: 0.02, 0.21 kg/m[superscript 2]. Similar associations were seen for reallocation of sedentary time in non-bouts to MVPA. Reallocating sedentary time in bouts to LPA was associated only with lower waist circumference.
Conclusion
Reallocation of sedentary time in bouts as well as non-bouts to MVPA, but not to LPA, was beneficially associated with waist circumference, BMI and HDL cholesterol in individuals with prediabetes and type 2 diabetes. The results of this study confirm the importance of reallocation sedentary time to MVPA.
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.