RÁZGA, Filip, Jaroslav KOČA, Ali MOKDAD a Jiří ŠPONER. Elastic properties of ribosomal RNA building blocks: molecular dynamics of the GTPase-associated center rRNA. Nucleic Acids Research. Oxford, UK: Oxford Press, 2007, roč. 35, č. 12, s. 4007–4017. ISSN 0305-1048.
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Základní údaje
Originální název Elastic properties of ribosomal RNA building blocks: molecular dynamics of the GTPase-associated center rRNA
Název česky Elastické vlastnosti stavebných blokov ribozomálnej RNA: molekulová dynamika GTPase-associated center rRNA
Autoři RÁZGA, Filip (703 Slovensko), Jaroslav KOČA (203 Česká republika), Ali MOKDAD (840 Spojené státy) a Jiří ŠPONER (203 Česká republika, garant).
Vydání Nucleic Acids Research, Oxford, UK, Oxford Press, 2007, 0305-1048.
Další údaje
Originální jazyk angličtina
Typ výsledku Článek v odborném periodiku
Obor 10403 Physical chemistry
Stát vydavatele Velká Británie a Severní Irsko
Utajení není předmětem státního či obchodního tajemství
Impakt faktor Impact factor: 6.954
Kód RIV RIV/00216224:14310/07:00022189
Organizační jednotka Přírodovědecká fakulta
UT WoS 000247817700013
Klíčová slova anglicky Molecular Dynamics; RNA Kink Turn; Ribosome; RNA flexibility; RNA building blocks
Štítky molecular dynamics, Ribosome, RNA building blocks, RNA flexibility, RNA Kink Turn
Příznaky Mezinárodní význam
Změnil Změnil: prof. RNDr. Jiří Šponer, DrSc., učo 28764. Změněno: 18. 1. 2008 11:33.
Anotace
Explicit solvent Molecular Dynamics (MD) was used to describe the intrinsic flexibility of the Helix 42-44 portion of the 23S rRNA (abbreviated as Kt-42+rGAC; Kink-turn 42 and GTPase associated center rRNA). The bottom part of this molecule consists of alternating rigid and flexible segments. The first flexible segment (Hinge1) is the highly anharmonic Kink of Kt-42. The second one (Hinge2) is localized at the junction between Helix 42 and Helices 43/44. The rigid segments are the two arms of Helix 42 flanking the Kink. The whole molecule ends up with compact Helices 43/44 (Head) which appear to be modestly compressed towards the subunit in the H.m. x-ray structure. Overall, the Helix 42-44 rRNA is constructed as a sophisticated intrinsically flexible anisotropic molecular limb. The leading flexibility modes include bending at the hinges and twisting. The Head shows visible internal conformational plasticity, stemming from an intricate set of base pairing patterns including dynamical triads and tetrads. In summary, we demonstrate how rRNA building blocks with contrasting intrinsic flexibilities can form larger architectures with highly specific patterns of preferred low-energy motions and geometries.
Anotace česky
Explicit solvent Molecular Dynamics (MD) was used to describe the intrinsic flexibility of the Helix 42-44 portion of the 23S rRNA (abbreviated as Kt-42+rGAC; Kink-turn 42 and GTPase associated center rRNA). The bottom part of this molecule consists of alternating rigid and flexible segments. The first flexible segment (Hinge1) is the highly anharmonic Kink of Kt-42. The second one (Hinge2) is localized at the junction between Helix 42 and Helices 43/44. The rigid segments are the two arms of Helix 42 flanking the Kink. The whole molecule ends up with compact Helices 43/44 (Head) which appear to be modestly compressed towards the subunit in the H.m. x-ray structure. Overall, the Helix 42-44 rRNA is constructed as a sophisticated intrinsically flexible anisotropic molecular limb. The leading flexibility modes include bending at the hinges and twisting. The Head shows visible internal conformational plasticity, stemming from an intricate set of base pairing patterns including dynamical triads and tetrads. In summary, we demonstrate how rRNA building blocks with contrasting intrinsic flexibilities can form larger architectures with highly specific patterns of preferred low-energy motions and geometries.
Návaznosti
LC06030, projekt VaVNázev: Biomolekulární centrum
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum
MSM0021622413, záměrNázev: 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
VytisknoutZobrazeno: 26. 4. 2024 23:26