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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F05%3A00014133%21RIV10-MSM-14310___
rdf:type
skos:Concept n9:Vysledek
dcterms:description
One of the objectives of protein engineering is to propose and construct modified enzymes with improved catalytic activity for substrate of interest. The rational engineering of an enzyme requires to know which amino acid residues of the protein are involved in the catalysis and how to modify them to achieve an increased activity. The program TRITON is a graphical tool for modelling protein mutants and assessment of their activities [1,2]. Protein mutants are modelled based on the wild type structure by homology modelling using the external program MODELLER. Enzymatic reactions taking place in the mutants active site are modelled using the semi-empirical quantum mechanic program MOPAC. Activities of the mutants can be estimated by evaluation the changes in energies of the system and partial atomic charges of the active site residues during the reaction. The program TRITON offers graphical tools for preparation of input data files, for calculation and for the analysis of generated output data. One of the objectives of protein engineering is to propose and construct modified enzymes with improved catalytic activity for substrate of interest. The rational engineering of an enzyme requires to know which amino acid residues of the protein are involved in the catalysis and how to modify them to achieve an increased activity. The program TRITON is a graphical tool for modelling protein mutants and assessment of their activities [1,2]. Protein mutants are modelled based on the wild type structure by homology modelling using the external program MODELLER. Enzymatic reactions taking place in the mutants active site are modelled using the semi-empirical quantum mechanic program MOPAC. Activities of the mutants can be estimated by evaluation the changes in energies of the system and partial atomic charges of the active site residues during the reaction. The program TRITON offers graphical tools for preparation of input data files, for calculation and for the analysis of generated output data.
dcterms:title
TRITON: graphic software for modelling protein mutants and calculation reaction pathways TRITON: graphic software for modelling protein mutants and calculation reaction pathways
skos:prefLabel
TRITON: graphic software for modelling protein mutants and calculation reaction pathways TRITON: graphic software for modelling protein mutants and calculation reaction pathways
skos:notation
RIV/00216224:14310/05:00014133!RIV10-MSM-14310___
n4:aktivita
n7:Z
n4:aktivity
Z(MSM0021622413)
n4:dodaniDat
n8:2010
n4:domaciTvurceVysledku
n14:4347374 n14:1030175 n14:3993779
n4:druhVysledku
n16:D
n4:duvernostUdaju
n5:S
n4:entitaPredkladatele
n11:predkladatel
n4:idSjednocenehoVysledku
547340
n4:idVysledku
RIV/00216224:14310/05:00014133
n4:jazykVysledku
n10:eng
n4:klicovaSlova
protein; mutant; reaction; pathway; TRITON
n4:klicoveSlovo
n15:pathway n15:mutant n15:protein n15:TRITON n15:reaction
n4:kontrolniKodProRIV
[C310AD496F64]
n4:mistoKonaniAkce
Nove Hrady
n4:mistoVydani
Praha
n4:nazevZdroje
Materials Structure in Chemistry, Biology, Physics and Technology
n4:obor
n13:CF
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
3
n4:rokUplatneniVysledku
n8:2005
n4:tvurceVysledku
Prokop, Martin Damborský, Jiří Koča, Jaroslav
n4:typAkce
n17:CST
n4:zahajeniAkce
2005-01-01+01:00
n4:zamer
n20:MSM0021622413
s:issn
1211-5894
s:numberOfPages
1
n19:hasPublisher
Czech and Slovak Crystallographic Association
n18:organizacniJednotka
14310