| RÉBLOVÁ, Kamila, Filip LANKAŠ, Filip RÁZGA, Maryna V KRASOVSKA, Jaroslav KOČA and Jiří ŠPONER. Structure, Dynamics, and Elasticity of Free 16S rRNA Helix 44 Studied by Molecular Dynamics Simulations. Biopolymers. USA: Wiley InterScience, 2006, vol. 82, No 5, p. 504-520. ISSN 0006-3525. |
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@article{691351,
author = {Réblová, Kamila and Lankaš, Filip and Rázga, Filip and Krasovska, Maryna V and Koča, Jaroslav and Šponer, Jiří},
article_location = {USA},
article_number = {5},
keywords = {Molecular dynamics; elasticity; Helix 44},
language = {eng},
issn = {0006-3525},
journal = {Biopolymers},
title = {Structure, Dynamics, and Elasticity of Free 16S rRNA Helix 44 Studied by Molecular Dynamics Simulations},
volume = {82},
year = {2006}
}
TY - JOUR
ID - 691351
AU - Réblová, Kamila - Lankaš, Filip - Rázga, Filip - Krasovska, Maryna V - Koča, Jaroslav - Šponer, Jiří
PY - 2006
TI - Structure, Dynamics, and Elasticity of Free 16S rRNA Helix 44 Studied by Molecular Dynamics Simulations
JF - Biopolymers
VL - 82
IS - 5
SP - 504-520
EP - 504-520
PB - Wiley InterScience
SN - 00063525
KW - Molecular dynamics
KW - elasticity
KW - Helix 44
N2 - Molecular dynamics simulations were employed to investigate the structure, dynamics, and local base-pair deformability of the free 16S ribosomal helix 44 from Thermus thermophilus and of a canonical A-RNA double helix. While helix 44 is bent in the crystal structure of the small ribosomal subunit, the simulated helix 44 is intrinsically straight. It shows, however, substantial instantaneous bends that are isotropic. The spontaneous motions seen in simulations achieve large degrees of bending seen in the X-ray structure and would be entirely sufficient to allow the dynamics of the upper part of helix 44 evidenced by cryo-electron microscopy studies. Analysis of local base-pair step deformability reveals a patch of flexible steps in the upper part of helix 44 and in the area proximal to the bulged bases, suggesting that the upper part of helix 44 has enhanced flexibility. The simulations identify two conformational substates of the second bulge area (bottom part of the helix) with distinct base pairing. In agreement with NMR and X-ray studies, a flipped out conformational substate of conserved 1492A is seen in the first bulge area.
ER -
RÉBLOVÁ, Kamila, Filip LANKAŠ, Filip RÁZGA, Maryna V KRASOVSKA, Jaroslav KOČA and Jiří ŠPONER. Structure, Dynamics, and Elasticity of Free 16S rRNA Helix 44 Studied by Molecular Dynamics Simulations. \textit{Biopolymers}. USA: Wiley InterScience, 2006, vol.~82, No~5, p.~504-520. ISSN~0006-3525.
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