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PERMOL : restraint-based protein homology modeling using DYANA or CNS

Title data

Möglich, Andreas ; Weinfurtner, Daniel ; Gronwald, Wolfram ; Maurer, Till ; Kalbitzer, Hans Robert:
PERMOL : restraint-based protein homology modeling using DYANA or CNS.
In: Bioinformatics. Vol. 21 (2005) Issue 9 . - pp. 2110-2111.
ISSN 1367-4803
DOI: https://doi.org/10.1093/bioinformatics/bti276

Abstract in another language

SUMMARY

PERMOL is a new restraint-based program for homology modeling of proteins. Restraints are generated from the information contained in structures of homologous template proteins. Employing the restraints generated by PERMOL, three-dimensional structures are obtained using MD programs such as DYANA or CNS. In contrast to other programs PERMOL is mainly based on the use of dihedral angle information which is optimally suited to preserve the local secondary structure. The global arrangement of these elements is then facilitated by a small number of distance restraints. Using PERMOL homology, models of high quality are obtained. A key advantage of the proposed method is its flexibility, which allows the inclusion of data from other sources, such as experimental restraints and the use of modern molecular dynamics programs to calculate structures.

AVAILABILITY

The software and a detailed manual are available free of charge (http://www.biologie.uni-regensburg.de/Biophysik/Kalbitzer/permol/permol.html)

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 15671120
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 20 May 2015 07:10
Last Modified: 21 Apr 2022 13:39
URI: https://eref.uni-bayreuth.de/id/eprint/13614