<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kulkarni, Aarohi</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Biochemical characterization of an aspartic protease from vigna radiata: kinetic interactions with the classical inhibitor pepstatin implicating a tight binding mechanism</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica Et Biophysica Acta-Proteins and Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ant colony</style></keyword><keyword><style  face="normal" font="default" size="100%">global optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">metaheuristics</style></keyword><keyword><style  face="normal" font="default" size="100%">multimodal continuous functions</style></keyword><keyword><style  face="normal" font="default" size="100%">particle swarm optimization</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE INC</style></publisher><pub-location><style face="normal" font="default" size="100%">360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA</style></pub-location><volume><style face="normal" font="default" size="100%">1774</style></volume><pages><style face="normal" font="default" size="100%">619-627</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;{Aspartic proteases are the focus of recent research interest in understanding the physiological importance of this class of enzymes in plants. This is the first report of an aspartic protease from the seeds of Vigna radiata. The aspartic protease was purified to homogeneity by fractional ammonium sulfate precipitation and pepstatin-A agarose affinity column. It was found to have a molecular weight of 67,406 Da by gel filtration chromatography. SDS-PAGE analysis revealed the presence of a heterodimer with subunits of molecular weights of 44,024 and 23,349 Da respectively. The enzyme was pH stable with the amino acid analysis confirming the molecular weight of the protein. The substrate cleavage site as analyzed by using the synthetic substrate was found to be the Phe-Tyr bond. The kinetic interactions of the enzyme were studied with the universal inhibitor, pepstatin A. This is the first report on the interactions of a plant aspartic protease with pepstatin-A, an inhibitor from a microbial source. A competitive one-step mechanism of binding is observed. The progress curves are time-dependent and consistent with tight binding inhibition. The K(i) value of the reversible complex of pepstatin with the enzyme was 0.87 mu M whereas the overall inhibition constant K(i)*&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;2.747&lt;/p&gt;</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shelokar, P. S.</style></author><author><style face="normal" font="default" size="100%">Jayaraman, Valadi K.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, B. D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multicanonical jump walk annealing assisted by tabu for dynamic optimization of chemical engineering processes</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Operational Research</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dynamic optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">metaheuristics</style></keyword><keyword><style  face="normal" font="default" size="100%">Monte Carlo simulations</style></keyword><keyword><style  face="normal" font="default" size="100%">multicanonical algorithms</style></keyword><keyword><style  face="normal" font="default" size="100%">simulated annealing</style></keyword><keyword><style  face="normal" font="default" size="100%">tabu conditions</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">185</style></volume><pages><style face="normal" font="default" size="100%">1213-1229</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A hybrid methodology, viz., multicanonical jump walk annealing assisted by tabu list (MJWAT) is proposed for solving dynamic optimization problems in chemically reacting systems. This method combines the power of multicanonical sampling with the beneficial features of simulated annealing. Incorporating tabu list further enhances the efficiency of the method. The superior performance of the MJWAT is highlighted with the help of five benchmark case studies. (C) 2006 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.158</style></custom4></record></records></xml>