@article{harris_epting_kelly_2010, title={N-terminal Fusion of a Hyperthermophilic Chitin-Binding Domain to Xylose Isomerase from Thermotoga neapolitana Enhances Kinetics and Thermostability of Both Free and Immobilized Enzymes}, volume={26}, ISSN={["1520-6033"]}, DOI={10.1002/btpr.416}, abstractNote={Abstract}, number={4}, journal={BIOTECHNOLOGY PROGRESS}, author={Harris, James M. and Epting, Kevin L. and Kelly, Robert M.}, year={2010}, pages={993–1000} }
 @article{kaczowka_madding_epting_kelly_cianciolo_pizzo_2008, title={Probing the stability of native and activated forms of alpha(2)-macroglobulin}, volume={42}, ISSN={["0141-8130"]}, DOI={10.1016/j.ijbiomac.2007.09.019}, abstractNote={α2-Macroglobulin (α2M) is a 718 kDa homotetrameric proteinase inhibitor which undergoes a large conformational change upon activation. This conformational change can occur either by proteolytic attack on an ∼40 amino acid stretch, the bait region, which results in the rupture of the four thioester bonds in α2M, or by direct nucleophilic attack on these thioesters by primary amines. Amine activation circumvents both bait region cleavage and protein incorporation, which occurs by proteolytic activation. These different activation methods allow for examination of the roles bait region cleavage and thioester rupture play in α2M stability. Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of α2M complexes.}, number={1}, journal={INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES}, author={Kaczowka, Steven J. and Madding, Lara S. and Epting, Kevin L. and Kelly, Robert M. and Cianciolo, George J. and Pizzo, Salvatore V.}, year={2008}, month={Jan}, pages={62–67} }
 @article{madding_michel_shockley_conners_epting_johnson_kelly_2007, title={Role of the beta 1 subunit in the function and stability of the 20S proteasome in the hyperthermophilic archaeon Pyrococcus furiosus}, volume={189}, ISSN={["0021-9193"]}, DOI={10.1128/JB.01382-06}, abstractNote={ABSTRACT}, number={2}, journal={JOURNAL OF BACTERIOLOGY}, author={Madding, Lara S. and Michel, Joshua K. and Shockley, Keith R. and Conners, Shannon B. and Epting, Kevin L. and Johnson, Matthew R. and Kelly, Robert M.}, year={2007}, month={Jan}, pages={583–590} }
 @article{mcguffey_epting_kelly_foegeding_2005, title={Denaturation and aggregation of three alpha-lactalbumin preparations at neutral pH}, volume={53}, ISSN={["1520-5118"]}, DOI={10.1021/jf048863p}, abstractNote={The denaturation and aggregation of reagent-grade (Sigmaalpha-La), ion-exchange chromatography purified (IEXalpha-La), and a commercial-grade (Calpha-La) alpha-lactalbumin were studied with differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, and turbidity measurement. All three preparations had similar thermal denaturation temperatures with an average of 63.7 degrees C. Heating pure preparations of alpha-lactalbumin produced three non-native monomer species and three distinct dimer species. This phenomenon was not observed in Calpha-La. Turbidity development at 95 degrees C (tau95 degrees C) indicated that pure preparations rapidly aggregate at pH 7.0, and evidence suggests that hydrophobic interactions drove this phenomenon. The Calpha-La required 4 times the phosphate or excess Ca2+ concentrations to develop a similar tau95 degrees C to the pure preparations and displayed a complex pH-dependent tau95 degrees C behavior. Turbidity development dramatically decreased when the heating temperature was below 95 degrees C. A mechanism is provided, and the interrelationship between specific electrostatic interactions and hydrophobic attraction, in relation to the formation of disulfide-bonded products, is discussed.}, number={8}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={McGuffey, MK and Epting, KL and Kelly, RM and Foegeding, EA}, year={2005}, month={Apr}, pages={3182–3190} }
 @article{epting_vieille_zeikus_kelly_kelly_zeikus_vieille_2005, title={Influence of divalent cations on the structural thermostability and thermal inactivation kinetics of class II xylose isomerases}, volume={272}, ISSN={["1742-4658"]}, DOI={10.1111/j.1742-4658.2005.04577.x}, abstractNote={The effects of divalent metal cations on structural thermostability and the inactivation kinetics of homologous class II d‐xylose isomerases (XI; EC 5.3.1.5) from mesophilic (Escherichia coli and Bacillus licheniformis), thermophilic (Thermoanaerobacterium thermosulfurigenes), and hyperthermophilic (Thermotoga neapolitana) bacteria were examined. Unlike the three less thermophilic XIs that were substantially structurally stabilized in the presence of Co2+ or Mn2+ (and Mg2+ to a lesser extent), the melting temperature [(Tm) ≈100 °C] of T. neapolitana XI (TNXI) varied little in the presence or absence of a single type of metal. In the presence of any two of these metals, TNXI exhibited a second melting transition between 110 °C and 114 °C. TNXI kinetic inactivation, which was non‐first order, could be modeled as a two‐step sequential process. TNXI inactivation in the presence of 5 mm metal at 99–100 °C was slowest in the presence of Mn2+[half‐life (t1/2) of 84 min], compared to Co2+ (t1/2 of 14 min) and Mg2+ (t1/2 of 2 min). While adding Co2+ to Mg2+ increased TNXI's t1/2 at 99–100 °C from 2 to 7.5 min, TNXI showed no significant activity at temperatures above the first melting transition. The results reported here suggest that, unlike the other class II XIs examined, single metals are required for TNXI activity, but are not essential for its structural thermostability. The structural form corresponding to the second melting transition of TNXI in the presence of two metals is not known, but likely results from cooperative interactions between dissimilar metals in the two metal binding sites.}, number={6}, journal={FEBS JOURNAL}, author={Epting, KL and Vieille, C and Zeikus, JG and Kelly, RM and Kelly, RM and Zeikus, JG and Vieille, C}, year={2005}, month={Mar}, pages={1454–1464} }
 @article{bandlish_hess_epting_vieille_kelly_2002, title={Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species}, volume={80}, ISSN={["0006-3592"]}, DOI={10.1002/bit.10362}, abstractNote={Abstract}, number={2}, journal={BIOTECHNOLOGY AND BIOENGINEERING}, author={Bandlish, RK and Hess, JM and Epting, KL and Vieille, C and Kelly, RM}, year={2002}, month={Oct}, pages={185–194} }