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Prediction of folding nuclei in tRNA molecules. / Pereyaslavets, L. B.; Baranov, M. V.; Leonova, E. I.; Galzitskaya, O. V.

In: Biochemistry (Moscow), Vol. 76, No. 2, 01.02.2011, p. 236-244.

Research output: Contribution to journal › Article › peer-review

Harvard

Pereyaslavets, LB, Baranov, MV, Leonova, EI & Galzitskaya, OV 2011, 'Prediction of folding nuclei in tRNA molecules', Biochemistry (Moscow), vol. 76, no. 2, pp. 236-244. https://doi.org/10.1134/S0006297911020106

APA

Pereyaslavets, L. B., Baranov, M. V., Leonova, E. I., & Galzitskaya, O. V. (2011). Prediction of folding nuclei in tRNA molecules. Biochemistry (Moscow), 76(2), 236-244. https://doi.org/10.1134/S0006297911020106

Vancouver

Pereyaslavets LB, Baranov MV, Leonova EI, Galzitskaya OV. Prediction of folding nuclei in tRNA molecules. Biochemistry (Moscow). 2011 Feb 1;76(2):236-244. https://doi.org/10.1134/S0006297911020106

Author

Pereyaslavets, L. B. ; Baranov, M. V. ; Leonova, E. I. ; Galzitskaya, O. V. / Prediction of folding nuclei in tRNA molecules. In: Biochemistry (Moscow). 2011 ; Vol. 76, No. 2. pp. 236-244.

BibTeX

@article{735f9617403445cf95d1be99d01b6b5e,
title = "Prediction of folding nuclei in tRNA molecules",
abstract = "Prediction of folding nuclei in RNA molecules allows one to look in a new way at the problem of possible RNA base sequence folding and at problems associated with incorrect RNA folding, as well as at RNA structure stability. We have chosen a model and energy parameters for description of RNA structure. The algorithm for studying processes including protein folding/unfolding was successfully applied to calculations on tRNA. Four tRNA molecules were considered whose structures were obtained in the free state (tRNA Phe, tRNA Asp, tRNA fMet, and tRNA Lys). The calculated Φ-values for tRNA molecules correlate with experimental data showing that nucleotide residues in the D and T hairpin regions are involved in tRNA structure last, or more exactly, they are not included in the tRNA folding nucleus. High Φ-values in the anticodon hairpin region show that the nucleus of tRNA folding is localized just in that place.",
keywords = "coarse-grained structural model, Dynamic programming, folding nucleus, hydrogen bond, stacking and hydrophobic interactions, tRNA folding",
author = "Pereyaslavets, {L. B.} and Baranov, {M. V.} and Leonova, {E. I.} and Galzitskaya, {O. V.}",
year = "2011",
month = feb,
day = "1",
doi = "10.1134/S0006297911020106",
language = "English",
volume = "76",
pages = "236--244",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "2",

}

RIS

TY - JOUR

T1 - Prediction of folding nuclei in tRNA molecules

AU - Pereyaslavets, L. B.

AU - Baranov, M. V.

AU - Leonova, E. I.

AU - Galzitskaya, O. V.

PY - 2011/2/1

Y1 - 2011/2/1

N2 - Prediction of folding nuclei in RNA molecules allows one to look in a new way at the problem of possible RNA base sequence folding and at problems associated with incorrect RNA folding, as well as at RNA structure stability. We have chosen a model and energy parameters for description of RNA structure. The algorithm for studying processes including protein folding/unfolding was successfully applied to calculations on tRNA. Four tRNA molecules were considered whose structures were obtained in the free state (tRNA Phe, tRNA Asp, tRNA fMet, and tRNA Lys). The calculated Φ-values for tRNA molecules correlate with experimental data showing that nucleotide residues in the D and T hairpin regions are involved in tRNA structure last, or more exactly, they are not included in the tRNA folding nucleus. High Φ-values in the anticodon hairpin region show that the nucleus of tRNA folding is localized just in that place.

AB - Prediction of folding nuclei in RNA molecules allows one to look in a new way at the problem of possible RNA base sequence folding and at problems associated with incorrect RNA folding, as well as at RNA structure stability. We have chosen a model and energy parameters for description of RNA structure. The algorithm for studying processes including protein folding/unfolding was successfully applied to calculations on tRNA. Four tRNA molecules were considered whose structures were obtained in the free state (tRNA Phe, tRNA Asp, tRNA fMet, and tRNA Lys). The calculated Φ-values for tRNA molecules correlate with experimental data showing that nucleotide residues in the D and T hairpin regions are involved in tRNA structure last, or more exactly, they are not included in the tRNA folding nucleus. High Φ-values in the anticodon hairpin region show that the nucleus of tRNA folding is localized just in that place.

KW - coarse-grained structural model

KW - Dynamic programming

KW - folding nucleus

KW - hydrogen bond

KW - stacking and hydrophobic interactions

KW - tRNA folding

UR - http://www.scopus.com/inward/record.url?scp=79953850355&partnerID=8YFLogxK

U2 - 10.1134/S0006297911020106

DO - 10.1134/S0006297911020106

M3 - Article

C2 - 21568857

AN - SCOPUS:79953850355

VL - 76

SP - 236

EP - 244

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 2

ER -

ID: 45420199