Detailed Information on Publication Record
2007
Computational study of restriction endonuclease HincII
FADRNÁ, Eva, Jiří FUKAL and Jaroslav KOČABasic information
Original name
Computational study of restriction endonuclease HincII
Name in Czech
Počítačové studium restrikční endonukleasy HincII
Authors
FADRNÁ, Eva, Jiří FUKAL and Jaroslav KOČA
Edition
Nové Hrady, Czech Republic, Materials Structure, vol. 14, no. 1 (2007), 6th Discussions in Structural Molecular Biology, p. 33-33, 1 pp. 2007
Publisher
Academic and University Center, Nové Hrady
Other information
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
Keywords in English
molecular modeling; restriction endonuclease; HincII
Tags
International impact
Změněno: 16/1/2008 09:35, Mgr. Eva Fadrná, Ph.D.
V originále
We have examined the stability and/or dynamics of protein/DNA complex HincII by computational tools. Although molecular dynamics is not able to follow the reaction mechanism itself, it may serve as a good tool to describe reaction partners or intermediates. We want to describe the structure of the complex to provide detailed view of the active site and relationships in it. The stability of the ions coordination can be seen from our simulations, as well as electrostatics around them. We attempt to bring some ideas about the structure of the active site and possible role of the ions in it. We have found strong electrostatic potential around catalytic aminoacids, which is ballanced by presence of ions. It leads to the idea that B site ion is required at least to stabilize the reaction environment.
In Czech
We have examined the stability and/or dynamics of protein/DNA complex HincII by computational tools. Although molecular dynamics is not able to follow the reaction mechanism itself, it may serve as a good tool to describe reaction partners or intermediates. We want to describe the structure of the complex to provide detailed view of the active site and relationships in it. The stability of the ions coordination can be seen from our simulations, as well as electrostatics around them. We attempt to bring some ideas about the structure of the active site and possible role of the ions in it. We have found strong electrostatic potential around catalytic aminoacids, which is ballanced by presence of ions. It leads to the idea that B site ion is required at least to stabilize the reaction environment.
Links
| MSM0021622413, plan (intention) |
|