TRITON: graphic software for modelling protein mutants and calculation reaction pathways

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00014133" target="_blank" >RIV/00216224:14310/05:00014133 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

TRITON: graphic software for modelling protein mutants and calculation reaction pathways

Original language 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 byhomology 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 outpu

Czech name

TRITON: graficky program pro modelovani proteinovych mutantu a vypocet reakcnich cest

Czech 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 byhomology 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 outpu

Type

D - Article in proceedings

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2005

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection

Materials Structure in Chemistry, Biology, Physics and Technology

ISBN

1211-5894

ISSN

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e-ISSN

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Number of pages

1

Pages from-to

17

Publisher name

Czech and Slovak Crystallographic Association

Place of publication

Praha

Event location

Nove Hrady

Event date

Jan 1, 2005

Type of event by nationality

CST - Celostátní akce

UT code for WoS article

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