TUTCRIS - Tampereen teknillinen yliopisto

TUTCRIS

Urea and guanidinium induced denaturation of a Trp-cage miniprotein

Tutkimustuotosvertaisarvioitu

Standard

Urea and guanidinium induced denaturation of a Trp-cage miniprotein. / Heyda, Jan; Kožíšek, Milan; Bednárova, Lucie; Thompson, Gary; Konvalinka, Jan; Vondrášek, Jiří; Jungwirth, Pavel.

julkaisussa: Journal of Physical Chemistry Part B, Vuosikerta 115, Nro 28, 21.07.2011, s. 8910-8924.

Tutkimustuotosvertaisarvioitu

Harvard

Heyda, J, Kožíšek, M, Bednárova, L, Thompson, G, Konvalinka, J, Vondrášek, J & Jungwirth, P 2011, 'Urea and guanidinium induced denaturation of a Trp-cage miniprotein', Journal of Physical Chemistry Part B, Vuosikerta. 115, Nro 28, Sivut 8910-8924. https://doi.org/10.1021/jp200790h

APA

Heyda, J., Kožíšek, M., Bednárova, L., Thompson, G., Konvalinka, J., Vondrášek, J., & Jungwirth, P. (2011). Urea and guanidinium induced denaturation of a Trp-cage miniprotein. Journal of Physical Chemistry Part B, 115(28), 8910-8924. https://doi.org/10.1021/jp200790h

Vancouver

Heyda J, Kožíšek M, Bednárova L, Thompson G, Konvalinka J, Vondrášek J et al. Urea and guanidinium induced denaturation of a Trp-cage miniprotein. Journal of Physical Chemistry Part B. 2011 heinä 21;115(28):8910-8924. https://doi.org/10.1021/jp200790h

Author

Heyda, Jan ; Kožíšek, Milan ; Bednárova, Lucie ; Thompson, Gary ; Konvalinka, Jan ; Vondrášek, Jiří ; Jungwirth, Pavel. / Urea and guanidinium induced denaturation of a Trp-cage miniprotein. Julkaisussa: Journal of Physical Chemistry Part B. 2011 ; Vuosikerta 115, Nro 28. Sivut 8910-8924.

Bibtex - Lataa

@article{94868fa2e86c4f0fb51e8ecdea94cbae,
title = "Urea and guanidinium induced denaturation of a Trp-cage miniprotein",
abstract = "Using a combination of experimental techniques (circular dichroism, differential scanning calorimetry, and NMR) and molecular dynamics simulations, we performed an extensive study of denaturation of the Trp-cage miniprotein by urea and guanidinium. The experiments, despite their different sensitivities to various aspects of the denaturation process, consistently point to simple, two-state unfolding process. Microsecond molecular dynamics simulations with a femtosecond time resolution allow us to unravel the detailed molecular mechanism of Trp-cage unfolding. The process starts with a destabilizing proline shift in the hydrophobic core of the miniprotein, followed by a gradual destruction of the hydrophobic loop and the α-helix. Despite differences in interactions of urea vs guanidinium with various peptide moieties, the overall destabilizing action of these two denaturants on Trp-cage is very similar.",
author = "Jan Heyda and Milan Kož{\'i}šek and Lucie Bedn{\'a}rova and Gary Thompson and Jan Konvalinka and Jiř{\'i} Vondr{\'a}šek and Pavel Jungwirth",
year = "2011",
month = "7",
day = "21",
doi = "10.1021/jp200790h",
language = "English",
volume = "115",
pages = "8910--8924",
journal = "Journal of Physical Chemistry Part B",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "28",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Urea and guanidinium induced denaturation of a Trp-cage miniprotein

AU - Heyda, Jan

AU - Kožíšek, Milan

AU - Bednárova, Lucie

AU - Thompson, Gary

AU - Konvalinka, Jan

AU - Vondrášek, Jiří

AU - Jungwirth, Pavel

PY - 2011/7/21

Y1 - 2011/7/21

N2 - Using a combination of experimental techniques (circular dichroism, differential scanning calorimetry, and NMR) and molecular dynamics simulations, we performed an extensive study of denaturation of the Trp-cage miniprotein by urea and guanidinium. The experiments, despite their different sensitivities to various aspects of the denaturation process, consistently point to simple, two-state unfolding process. Microsecond molecular dynamics simulations with a femtosecond time resolution allow us to unravel the detailed molecular mechanism of Trp-cage unfolding. The process starts with a destabilizing proline shift in the hydrophobic core of the miniprotein, followed by a gradual destruction of the hydrophobic loop and the α-helix. Despite differences in interactions of urea vs guanidinium with various peptide moieties, the overall destabilizing action of these two denaturants on Trp-cage is very similar.

AB - Using a combination of experimental techniques (circular dichroism, differential scanning calorimetry, and NMR) and molecular dynamics simulations, we performed an extensive study of denaturation of the Trp-cage miniprotein by urea and guanidinium. The experiments, despite their different sensitivities to various aspects of the denaturation process, consistently point to simple, two-state unfolding process. Microsecond molecular dynamics simulations with a femtosecond time resolution allow us to unravel the detailed molecular mechanism of Trp-cage unfolding. The process starts with a destabilizing proline shift in the hydrophobic core of the miniprotein, followed by a gradual destruction of the hydrophobic loop and the α-helix. Despite differences in interactions of urea vs guanidinium with various peptide moieties, the overall destabilizing action of these two denaturants on Trp-cage is very similar.

UR - http://www.scopus.com/inward/record.url?scp=79960344032&partnerID=8YFLogxK

U2 - 10.1021/jp200790h

DO - 10.1021/jp200790h

M3 - Article

VL - 115

SP - 8910

EP - 8924

JO - Journal of Physical Chemistry Part B

JF - Journal of Physical Chemistry Part B

SN - 1520-6106

IS - 28

ER -