@article{(Open Science Index):https://publications.waset.org/pdf/10555,
	  title     = {Mutational Effect to Particular Interaction Energy of Cycloguanil Drug to Plasmodium Plasmodium Falciparum Dihydrofolate Reductase Enzymes},
	  author    = {A. Maitarad and  P. Maitarad},
	  country	= {},
	  institution	= {},
	  abstract     = {In order to find the particular interaction energy
between cylcloguanil and the amino acids surrounding the pocket of
wild type and quadruple mutant type PfDHFR enzymes, the MP2
method with basis set 6-31G(d,p) level of calculations was
performed. The obtained interaction energies found that Asp54 has
the strongest interaction energy to both wild type and mutant type of -
12.439 and -11.250 kcal/mol, respectively and three amino acids;
Asp54, Ile164 and Ile14 formed the H-bonding with cycloguanil
drug. Importantly, the mutation at Ser108Asn was the key important
of cycloguanil resistant with showing repulsive interaction energy.},
	    journal   = {International Journal of Pharmacological and Pharmaceutical Sciences},
	  volume    = {5},
	  number    = {4},
	  year      = {2011},
	  pages     = {160 - 163},
	  ee        = {https://publications.waset.org/pdf/10555},
	  url   	= {https://publications.waset.org/vol/52},
	  bibsource = {https://publications.waset.org/},
	  issn  	= {eISSN: 1307-6892},
	  publisher = {World Academy of Science, Engineering and Technology},
	  index 	= {Open Science Index 52, 2011},