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Structure development of the heat shock protein 27 by analyzing the evolutionary and functional relationships to other heat shock proteins

  • After the expression of the titin-Hsp27-construct with the following purification supplies no satisfied results which makes the realization of the atomic force microscopy not possible. The devel-opment of the structure model by using different bioinformatic methods can establish a model for the protein sequence. As bioinformatic methods the template search by different BLAST runs and free available software like SwissModel, Pcons, ModWeb and other tools are used. Nevertheless, the generated model is not the native conformation and has to be analyzed with other software until a stable conformation of the structure can be predicted. Depending on the time which is provided the generated model is a good approach for the aim this master thesis has.

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Metadaten
Author:Maria Beier
URN:urn:nbn:de:bsz:mit1-opus-24536
Document Type:Master's Thesis
Language:English
Date of Publication (online):2012/11/27
Publishing Institution:Hochschule Mittweida
Release Date:2012/11/27
GND Keyword:Hitzeschock-Proteine; Sequenzanalyse <Chemie>; Ligand <Biochemie>; Strukturmodell; Chemotherapie
Institutes:03 Mathematik / Naturwissenschaften / Informatik
Dewey Decimal Classification:570 Biowissenschaften, Biologie
Access Rights:Frei zugänglich
Licence (German):License LogoEs gilt das UrhG