@article {67},
	title = {Biochemical characterization of an aspartic protease from vigna radiata: kinetic interactions with the classical inhibitor pepstatin implicating a tight binding mechanism},
	journal = {Biochimica Et Biophysica Acta-Proteins and Proteomics},
	volume = {1774},
	number = {5},
	year = {2007},
	month = {MAY},
	pages = {619-627},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>{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)*</p>},
	keywords = {ant colony, global optimization, metaheuristics, multimodal continuous functions, particle swarm optimization},
	issn = {0096-3003},
	doi = {10.1016/j.bbapap.2007.03.014},
	author = {Kulkarni, Aarohi and Rao, Mala}
}
@article { ISI:000251070500021,
	title = {Multicanonical jump walk annealing assisted by tabu for dynamic optimization of chemical engineering processes},
	journal = {European Journal of Operational Research},
	volume = {185},
	number = {3},
	year = {2008},
	month = {MAR},
	pages = {1213-1229},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>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.</p>},
	keywords = {dynamic optimization, metaheuristics, Monte Carlo simulations, multicanonical algorithms, simulated annealing, tabu conditions},
	issn = {0377-2217},
	doi = {10.1016/j.ejor.2006.06.049},
	author = {Shelokar, P. S. and Jayaraman, Valadi K. and Kulkarni, B. D.}
}
