In silico solvation free energy and thermodynamics properties of H2S in cholinium-based amino acid ionic liquids

Using thermodynamic integration, we study the solvation free energy of 18 amino acid side chain equivalents in solvents with different polarities, ranging from the most polar water to the most non-polar cyclohexane.

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Comparative Study on Mitogen Activated Protein Kinase of Plasmodium Species by Using in silico Method

Scientific Research Journal ◽

10.24191/srj.v9i1.9411 ◽

2012 ◽

Vol 9 (1) ◽

pp. 1

Author(s):

Mohd Fakharul Zaman Raja Yahya ◽

Hasidah Mohd Sidek

Keyword(s):

Amino Acid ◽

In Silico ◽

Nuclear Export ◽

Nuclear Export Signal ◽

Plasmodium Species ◽

Mitogen Activated Protein Kinase ◽

Multiple Sequence ◽

Wide Range ◽

Mitogen Activated Protein ◽

Human Plasmodium

Malaria parasites, Plasmodium can infect a wide range of hosts including humans and rodents. There are two copies of mitogen activated protein kinases (MAPKs) in Plasmodium, namely MAPK1 and MAPK2. The MAPKs have been studied extensively in the human Plasmodium, P. falciparum. However, the MAPKs from other Plasmodium species have not been characterized and it is therefore the premise of presented study to characterize the MAPKs from other Plasmodium species-P. vivax, P. knowlesi, P. berghei, P. chabaudi and P.yoelli using a series of publicly available bioinformatic tools. In silico data indicates that all Plasmodium MAPKs are nuclear-localized and contain both a nuclear localization signal (NLS) and a Leucine-rich nuclear export signal (NES). The activation motifs of TDY and TSH were found to be fully conserved in Plasmodium MAPK1 and MAPK2, respectively. The detailed manual inspection of a multiple sequence alignment (MSA) construct revealed a total of 17 amino acid stack patterns comprising of different amino acids present in MAPKJ and MAPK2 respectively, with respect to rodent and human Plasmodia. It is proposed that these amino acid stack patterns may be useful in explaining the disparity between rodent and human Plasmodium MAPKs.

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Comparative Study on Mitogen Activated Protein Kinase of Plasmodium Species by Using In silico Method

Scientific Research Journal ◽

10.24191/srj.v9i1.5052 ◽

2012 ◽

Vol 9 (1) ◽

pp. 1

Author(s):

Mohd Fakharul Zaman Raja Yahya ◽

Hasidah Mohd Sidek

Keyword(s):

Amino Acid ◽

In Silico ◽

Nuclear Export ◽

Nuclear Export Signal ◽

Plasmodium Species ◽

Mitogen Activated Protein Kinase ◽

Multiple Sequence ◽

Bioinformatic Tools ◽

Wide Range ◽

Human Plasmodium

Malaria parasites, Plasmodium can infect a wide range ofhosts including humans and rodents. There are two copies ofmitogen activated protein kinases (MAPKs) in Plasmodium, namely MAPK1 and MAPK2. The MAPKs have been studied extensively in the human Plasmodium, P. falciparum. However, the MAPKs from other Plasmodium species have not been characterized and it is therefore the premise ofpresented study to characterize the MAPKs from other Plasmodium species-P. vivax, P. knowlesi, P. berghei, P. chabaudi and P.yoelli using a series ofpublicly available bioinformatic tools. In silico data indicates that all Plasmodium MAPKs are nuclear-localizedandcontain both a nuclear localization signal (NLS) anda Leucine-rich nuclear export signal (NES). The activation motifs ofTDYand TSH werefound to befully conserved in Plasmodium MAPK1 and MAPK2, respectively. The detailed manual inspection ofa multiple sequence alignment (MSA) construct revealed a total of 17 amino acid stack patterns comprising ofdifferent amino acids present in MAPK1 and MAPK2 respectively, with respect to rodent and human Plasmodia. 1t is proposed that these amino acid stack patterns may be useful in explaining the disparity between rodent and human Plasmodium MAPKs.

Download Full-text