![]() ![]() salt-bridges) to overall stability of halophilic proteins is yet to be understood. However, contribution of specific electrostatic interactions (i.e. Classical electrostatic stabilization was suggested as the key determinant for halophilic adaptation of protein. Halophilic proteins have greater abundance of acidic over basic and very low bulky hydrophobic residues. Nayek, Arnab Sen Gupta, Parth Sarthi Banerjee, Shyamashree Mondal, Buddhadev Bandyopadhyay, Amal K Salt-bridge energetics in halophilic proteins. Overall, our theoretical analyses provide insight into halophilic Interiors of proteins from halophiles are seen to possess relatively higher abundance of charge and polar side chains than that of mesophiles which seems to be satisfied by cooperative network salt-bridges. Recruitment of extensive network salt-bridges (46%) with a net contribution of −5.0 kcal mol−1 per salt-bridge, seems to be a halophilic design wherein favorable average contribution of background term (−10 kcal mol−1) exceeds than that of bridge term (−7 kcal mol−1). Greater desolvation penalty of these buried salt-bridges are counteracted by stable network salt-bridges apart from favorable equal contributions of bridge and background terms. Notably, 35% of salt-bridges in our database are buried and stable. Although, average contributions of component energy terms are equal, their individual details vary greatly from one another indicating their sensitivity to local micro-environment. Majority (78%) of salt-bridges in our dataset are stable and conserved in nature. Overall contributions of salt-bridges are −3.0 kcal mol−1. On average, 8 salt-bridges per 150 residues protein were observed which is almost twice than earlier report. We then perform extensive statistical analysis on general and energetic attributes on these salt-bridges. To understand this, we use Adaptive-Poison-Boltzmann-Solver Methods along with our home-built automation to workout net as well as associated component energy terms such as desolvation energy, bridge energy and background energy for 275 salt-bridges from 20 extremely halophilic proteins. Nayek, Arnab Sen Gupta, Parth Sarthi Banerjee, Shyamashree Mondal, Buddhadev Bandyopadhyay, Amal K. ![]() Salt-Bridge Energetics in Halophilic Proteins The temperature and solar insolation data when correlated with each of the MFCs average output current, revealed that both external factors have significant impact on MFC current output but the correlation coefficient varies from MFC to MFC depending on salt bridge dimensional parameters. Optimum combination was found at 260 mm salt bridge length and 506.7 mm2 cross sectional area with 4.75 mA of mean output current. Analysis of variance shows that salt bridge length has significant effect both on mean (with 53.90% contribution at 95% CL) and variance (with 56.46% contribution at 87% CL), whereas the effect of cross sectional area of the salt bridge and the interaction of these two factors is significant on mean only (with 95% CL). Trials were conducted for 3 days and output current of each of the MFCs along with solar insolation and atmospheric temperature were recorded. Nine MFCs were fabricated as per the nine trial conditions. An experiment has been designed using Taguchi L9 orthogonal array, taking length and cross sectional area of salt bridge as factors having three levels. Therefore, the main objective of this research is to investigate the effect of length and cross sectional area of salt bridge and the effect of solar radiation and atmospheric temperature on MFC current output. Many researchers who have studied and optimized various parameters related to salt bridge MFC, have not shed much light on the effect of salt bridge dimensional parameters on the MFC performance. One major problem of two chamber salt bridge microbial fuel cells (MFCs) is the high resistance offered by the salt bridge to anion flow. Sarma, Dhrupad Barua, Parimal Bakul Dey, Nabendu Nath, Sumitro Thakuria, Mrinmay Mallick, Synthia Investigation and Taguchi Optimization of Microbial Fuel Cell Salt Bridge Dimensional Parameters ![]()
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