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All Journal Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences Biota: Jurnal Ilmiah Ilmu-Ilmu Hayati
Muhammad Saifur Rohman
Laboratorium Biokimia Fakultas Kedokteran Universitas Brawijaya
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Environmental Science

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Konstruksi Open Reding Frames (ORF) Artifisial Berukuran 798-bp yang Menyandi Protein dengan Urutan Asam Amino Acak Prijambada, Irfan Dwidya; Al-Awally, Khotibul Umam; Rohman, Muhammad Saifur; Artama, Wayan
Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati Vol 9, No 1 (2004): February 2004
Publisher : Universitas Atma Jaya Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (221.472 KB) | DOI: 10.24002/biota.v9i1.2828

Abstract

Penyusunan pustaka dari open reading frames (ORF) buatan yang tersusun atas 798 bp (pasangan basa), 576  di antaranya tersusun secara acak, yang mampu menyandi 266 asam amino telah berhasil dilakukan. Dalam upaya penyusunan tersebut diperoleh 32 transforman,  lima di antaranya membawa ORF buatan. Dari kelima transforman yang membawa ORF buatan tersebut, hanya satu transforman yang mampu berekspresi dan menyandi suatu protein. Protein yang dihasilkan memiliki ukuran 17 kDa, berukuran lebih kecil daripada ukuran yang diharapkan yaitu 29 kDa.
Interaction Of Platelet Activating Factor Acetyl Hydrolase (Paf Ah) Enzyme In Gln281 To Arg281 Mutation Toward Paf And Its Molecular Dynamic Putri, Jayarani Fatimah; ., widodo; Rohman, Muhammad Saifur
Journal of Tropical Life Science Vol 4, No 1 (2014)
Publisher : Journal of Tropical Life Science

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Abstract

Platelet Activating Factor Acetyl Hydrolase (PAF AH) or LpPLA2 is key enzyme in myocardial infarction catalyzes the sn-2 acetyl group of Platelet Activating Factor (PAF) into lyso PAF and acetate as non-potent inflammatory molecules. PAF AH plays a critical role in arterial plaque development of Coronary Artery Disease (CAD). A crystal structure of PAF AH complexes with other ligand and effects of amino acid alteration to protein plasma consequence have also been reported. Here we report on the result of molecular docking and Molecular dynamic (MD) simulation carried out for PAF AH wild type (WT)/PAF and mutant Q281R/PAF complexes. Docking result shown that amino acid residues on active site of Q281 PAF AH mutant have not recognized on PAF AH. Eelectrostatics and hydrophobic bonds significantly reduced in Q281R than wild type. In the 7500 ps MD simulation Q281R showed less dynamics than WT but enzymatic machinary of mutant Q281R was not interrupted during MD simulation as well as PAF AH wildtype. These findings clearly indicated the importance effect of mutant Q281R in PAF AH recognition to its substrate
Co-Authors Al-Awally, Khotibul Umam Artama, Wayan Irfan Dwidya Prijambada Jamhari Jamhari Jayarani Fatimah Putri, Jayarani Fatimah