title: ANALISIS DINAMIKA MOLEKUL PROTEIN LYSOZYME PUTIH  TELUR DENGAN MODEL POTENSIAL LENNARD-JONES  MENGGUNAKAN APLIKASI GROMACS
creator: HARRY PRAYOGA, 1417041030
subject: 500 ilmu pengetahuan alam dan matematika
subject: 530 Fisika
description: Telah dilakukan analisis dinamika molekul protein lysozyme putih telur yang  diselimuti air bentuk kubik dengan variasi temperatur 300 K, 325 K, dan 350 K  serta melakukan perhitungan nilai energi potensial dengan persamaan Lennard  Jones yang dilakukan dengan aplikasi Gromacs. Pada temperatur 300 K  menunjukan nilai tekanan 2,54 bar dan nilai densitas 997,54 kg/m3 serta terjadi  perubahan unfolded state di rantai asam amino ARG21-CA dan SER81-CA yang  menghasilkan energi potensial 2992,14 kJ/mol. Pada temperatur 325 K  menunjukan nilai tekanan 4,84 bar dan nilai densitas 974 kg/m3 serta terjadi  perubahan unfolded state di rantai asam amino ASP101-CA dan GLN121-CA  yang menghasilkan energi potensial 2994,55 kJ/mol. Pada temperatur 350 K  menunjukan nilai tekanan 0,82 bar dan nilai densitas 948,747 kg/m3 serta terjadi  perubahan unfolded state di rantai asam amino ARG21-CA dan menghilangnya  rantai asam amino GLN121-CA yang menghasilkan energi potensial 2999,65  kJ/mol. Hasil Root Mean Standart Deviation (RMSD) menunjukan bahwa protein  mulai terdenaturasi pada temperatur 350 K yang ditandai pemutusan rantai asam  amino GLN121-CA sejauh 0.07 nm.  Kata kunci: dinamika molekul, Lennard-Jones, lysozyme, Gromacs.  The molecular dynamic analysis of lysozyme protein has been done using  Gromacs application. Lysozyme protein filled by water in the cubic form with  variation of temperature was 300 K, 325 K, and 350 K and calculated potential  energy values used Lennard Jones equation. Structure protein on temperature  was 300 K showed that pressure value was 2,54 bar and density value was 997,54  kg/m3  then protein changed in unfolded state on ARG21-CA and SER81-CA  amino acid chain with potential energy was 2992,14 kJ/mol . Structure protein on  temperature was 325 K showed that pressure value was 4,84 bar and density  value was 974 kg/m3    then protein changed in unfolded state on ASP101-CA and  GLN121-CA amino acid chain with potential energy was 2994,55 kJ/mol.  Structure protein on temperature was 350 K showed that pressure value was 0,82  bar and density value was 948,747 kg/m3    then protein changed in unfolded state  on ARG21-CA amino acid chain and lost on GLN121-CA amino acid chain with  potential energy was 2999,65 kJ/mol. Root Mean Standard Deviation (RMSD)  showed that the protein will be denaturated on temperature 350 K caused by lost  on GLN121-CA amino acid with distance was 0.07 nm.  Keywords: molecular dynamics, Lennard-Jones, lysozyme, Gromacs.
publisher: FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM
date: 2019
type: Skripsi
type: NonPeerReviewed
format: text
identifier: http://digilib.unila.ac.id/57470/1/ABSTRAK%20%28ABSTRACT%29.pdf
format: text
identifier: http://digilib.unila.ac.id/57470/2/SKRIPSI%20FULL.pdf
format: text
identifier: http://digilib.unila.ac.id/57470/3/SKRIPSI%20TANPA%20BAB%20PEMBAHASAN.pdf
identifier:   HARRY PRAYOGA, 1417041030  (2019) ANALISIS DINAMIKA MOLEKUL PROTEIN LYSOZYME PUTIH TELUR DENGAN MODEL POTENSIAL LENNARD-JONES MENGGUNAKAN APLIKASI GROMACS.  FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM, UNIVERSITAS LAMPUNG.     
relation: http://digilib.unila.ac.id/57470/