Computational study of restriction endonuclease HincII

FADRNÁ, Eva, Jiří FUKAL a Jaroslav KOČA. Computational study of restriction endonuclease HincII. In Materials Structure, vol. 14, no. 1 (2007), 6th Discussions in Structural Molecular Biology. Nové Hrady, Czech Republic: Academic and University Center, Nové Hrady. s. 33-33. 2007.

Základní údaje

• Originální název: Computational study of restriction endonuclease HincII
• Název česky: Počítačové studium restrikční endonukleasy HincII
• Autoři: FADRNÁ, Eva, Jiří FUKAL a Jaroslav KOČA.
• Vydání: Nové Hrady, Czech Republic, Materials Structure, vol. 14, no. 1 (2007), 6th Discussions in Structural Molecular Biology, od s. 33-33, 1 s. 2007.
• Nakladatel: Academic and University Center, Nové Hrady

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Stať ve sborníku
• Obor: 10600 1.6 Biological sciences
• Stát vydavatele: Česká republika
• Utajení: není předmětem státního či obchodního tajemství
• Organizační jednotka: Přírodovědecká fakulta
• Klíčová slova anglicky: molecular modeling; restriction endonuclease; HincII
• Štítky: HincII, molecular modeling, restriction endonuclease
• Příznaky: Mezinárodní význam

Anotace

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.

Anotace česky

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.

Návaznosti

• MSM0021622413, záměr: Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím