• Interdisciplinary Bio Central
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• v.1 no.1
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• pp.3.1-3.6
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• 2009

Introduction: GTPases known as translation factor play a vital role as ribosomal subunit assembly chaperone. The bacterial Obg proteins ($Spo{\underline{0B}}$-associated ${\underline{G}}TP$-binding protein) belong to the subfamily of P-loop GTPase proteins and now it is considered as one of the new target for antibacterial drug. The majority of bacterial Obgs have been commonly found to be associated with ribosome, implying that these proteins may play a fundamental role in ribosome assembly or maturation. In addition, one of the experimental evidences suggested that Bacillus subtilis Obg (BsObg) protein binds to the L13 ribosomal protein (BsL13) which is known to be one of the early assembly proteins of the 50S ribosomal subunit in Escherichia coli. In order to investigate binding mode between the BsObg and the BsL13, protein-protein docking simulation was carried out after generating 3D structure of the BsL13 structure using homology modeling method. Materials and Methods: Homology model structure of BsL13 was generated using the EcL13 crystal structure as a template. Protein-protein docking of BsObg protein with ribosomal protein BsL13 was performed by DOT, a macro-molecular docking software, in order to predict a reasonable binding mode. The solvated energy minimization calculation of the docked conformation was carried out to refine the structure. Results and Discussion: The possible binding conformation of BsL13 along with activated Obg fold in BsObg was predicted by computational docking study. The final structure is obtained from the solvated energy minimization. From the analysis, three important H-bond interactions between the Obg fold and the L13 were detected: Obg:Tyr27-L13:Glu32, Obg:Asn76-L13:Glu139, and Obg:Ala136-L13:Glu142. The interaction between the BsObg and BsL13 structures were also analyzed by electrostatic potential calculations to examine the interface surfaces. From the results, the key residues for hydrogen bonding and hydrophobic interaction between the two proteins were predicted. Conclusion and Prospects: In this study, we have focused on the binding mode of the BsObg protein with the ribosomal BsL13 protein. The interaction between the activated Obg and target protein was investigated with protein-protein docking calculations. The binding pattern can be further used as a base for structure-based drug design to find a novel antibacterial drug.

• Food Science and Preservation
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• v.24 no.2
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• pp.168-180
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• 2017

This study was performed to determine the rapid thawing method for reducing the thawing time of frozen pork loins and to examine the effects of supercooling on the microbiological, physicochemical, and sensory qualities of fresh and frozen-thawed pork during storage at -1.5, 4, and $15^{\circ}C$. Forced-air thawing at $4^{\circ}C$ was the most time-consuming process, whereas radio frequency thawing time was the shortest by dielectric heating. The supercooling storage temperature was chosen to be $-1.5^{\circ}C$ because microstructural damages were not observed in the pork sample after cooling at $-1.5^{\circ}C$ for 24 h. Fresh or frozen-thawed pork loins stored at $-1.5^{\circ}C$ had lower drip loss and total volatile base nitrogen, thiobarbituric acid-reactive substance, and Hunter b* levels than loins stored at 4 and $15^{\circ}C$. In addition, the least degree of increase in preexisting microorganisms counts of the fresh or frozen-thawed pork loin samples was obtained during supercooled storage at $-1.5^{\circ}C$. Sensory quality results of fresh and frozen-thawed pork loin samples stored at $-1.5^{\circ}C$ showed higher scores than the samples stored at 4 and $15^{\circ}C$. These data indicate that supercooling at $-1.5^{\circ}C$ in the meat processing industry would be effective for maintaining the quality of pork meats without ice crystal nucleation and formation.