Dynamics of RNA Kink-turns: Role of water molecules
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010007" target="_blank" >RIV/00216224:14310/04:00010007 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Dynamics of RNA Kink-turns: Role of water molecules
Original language description
Hinge-like RNA motifs called kink-turns occur at conserved positions in the 16S and 23S ribosomal RNAs.The presence of K-turns at key functional sites in the ribosome suggests that they confer flexibility to RNA protuberances that regulate the traversalof tRNAs from one binding site to another across the interface between the small and large subunit during protein synthesis cycle. We have carried out a set of explicit-solvent Molecular Dynamics (MD) simulations for selected K-turn motifs. The simulations indicate that K-turns are dynamically flexible, and thus capable of regulating significant inter-segmental motions. The simulations reveal specific long-residency hydration sites and monovalent counterions that stabilize non-Watson-Crick basepairs, sharp turns of the phosphodiester backbone and even mediate inter-segmental contacts. The implications for ribosome function will be discussed.
Czech name
Dynamika RNA Kink-turnov: uloha molekul vody
Czech description
Hinge-like RNA motifs called kink-turns occur at conserved positions in the 16S and 23S ribosomal RNAs.The presence of K-turns at key functional sites in the ribosome suggests that they confer flexibility to RNA protuberances that regulate the traversalof tRNAs from one binding site to another across the interface between the small and large subunit during protein synthesis cycle. We have carried out a set of explicit-solvent Molecular Dynamics (MD) simulations for selected K-turn motifs. The simulations indicate that K-turns are dynamically flexible, and thus capable of regulating significant inter-segmental motions. The simulations reveal specific long-residency hydration sites and monovalent counterions that stabilize non-Watson-Crick basepairs, sharp turns of the phosphodiester backbone and even mediate inter-segmental contacts. The implications for ribosome function will be discussed.
Classification
Type
D - Article in proceedings
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
American Chemical Society Division of Computers in Chemistry - Abstracts
ISBN
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ISSN
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e-ISSN
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Number of pages
1
Pages from-to
10
Publisher name
American Chemical Society
Place of publication
Washington
Event location
Anaheim, California, USA
Event date
Mar 28, 2004
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
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