Cold denaturation of the HIV-1 protease monomer

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Standard

Cold denaturation of the HIV-1 protease monomer. / Rösner, Heike Ilona; Caldarini, Martina; Prestel, Andreas; Vanoni, Maria Antonietta; Broglia, Ricardo Americo; Aliverti, Alessandro; Tiana, Guido; Kragelund, Birthe Brandt.

I: Biochemistry, Bind 56, Nr. 8, 07.02.2017, s. 1029-1032.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Rösner, HI, Caldarini, M, Prestel, A, Vanoni, MA, Broglia, RA, Aliverti, A, Tiana, G & Kragelund, BB 2017, 'Cold denaturation of the HIV-1 protease monomer', Biochemistry, bind 56, nr. 8, s. 1029-1032. https://doi.org/10.1021/acs.biochem.6b01141

APA

Rösner, H. I., Caldarini, M., Prestel, A., Vanoni, M. A., Broglia, R. A., Aliverti, A., Tiana, G., & Kragelund, B. B. (2017). Cold denaturation of the HIV-1 protease monomer. Biochemistry, 56(8), 1029-1032. https://doi.org/10.1021/acs.biochem.6b01141

Vancouver

Rösner HI, Caldarini M, Prestel A, Vanoni MA, Broglia RA, Aliverti A o.a. Cold denaturation of the HIV-1 protease monomer. Biochemistry. 2017 feb. 7;56(8):1029-1032. https://doi.org/10.1021/acs.biochem.6b01141

Author

Rösner, Heike Ilona ; Caldarini, Martina ; Prestel, Andreas ; Vanoni, Maria Antonietta ; Broglia, Ricardo Americo ; Aliverti, Alessandro ; Tiana, Guido ; Kragelund, Birthe Brandt. / Cold denaturation of the HIV-1 protease monomer. I: Biochemistry. 2017 ; Bind 56, Nr. 8. s. 1029-1032.

Bibtex

@article{72a272d577b8435eba65fe48379a08de,
title = "Cold denaturation of the HIV-1 protease monomer",
abstract = "The HIV-1-protease is a complex protein which in its active form adopts a homodimer dominated by -sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1-protease which is populated above 0ºC and therefore directly accessible to various spectroscopic approaches. From NMR secondary chemical shifts, temperature coefficients and protein dynamics we suggest that the cold denatured state populates a compact wet globule containing transient non-native-like -helical elements. From the linearity of the temperature coefficients and the hydrodynamic radii, we propose that the overall architecture of the cold-denatured state is maintained over the temperature range studied.",
keywords = "Journal Article",
author = "R{\"o}sner, {Heike Ilona} and Martina Caldarini and Andreas Prestel and Vanoni, {Maria Antonietta} and Broglia, {Ricardo Americo} and Alessandro Aliverti and Guido Tiana and Kragelund, {Birthe Brandt}",
year = "2017",
month = feb,
day = "7",
doi = "10.1021/acs.biochem.6b01141",
language = "English",
volume = "56",
pages = "1029--1032",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "8",

}

RIS

TY - JOUR

T1 - Cold denaturation of the HIV-1 protease monomer

AU - Rösner, Heike Ilona

AU - Caldarini, Martina

AU - Prestel, Andreas

AU - Vanoni, Maria Antonietta

AU - Broglia, Ricardo Americo

AU - Aliverti, Alessandro

AU - Tiana, Guido

AU - Kragelund, Birthe Brandt

PY - 2017/2/7

Y1 - 2017/2/7

N2 - The HIV-1-protease is a complex protein which in its active form adopts a homodimer dominated by -sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1-protease which is populated above 0ºC and therefore directly accessible to various spectroscopic approaches. From NMR secondary chemical shifts, temperature coefficients and protein dynamics we suggest that the cold denatured state populates a compact wet globule containing transient non-native-like -helical elements. From the linearity of the temperature coefficients and the hydrodynamic radii, we propose that the overall architecture of the cold-denatured state is maintained over the temperature range studied.

AB - The HIV-1-protease is a complex protein which in its active form adopts a homodimer dominated by -sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1-protease which is populated above 0ºC and therefore directly accessible to various spectroscopic approaches. From NMR secondary chemical shifts, temperature coefficients and protein dynamics we suggest that the cold denatured state populates a compact wet globule containing transient non-native-like -helical elements. From the linearity of the temperature coefficients and the hydrodynamic radii, we propose that the overall architecture of the cold-denatured state is maintained over the temperature range studied.

KW - Journal Article

U2 - 10.1021/acs.biochem.6b01141

DO - 10.1021/acs.biochem.6b01141

M3 - Journal article

C2 - 28168877

VL - 56

SP - 1029

EP - 1032

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 8

ER -

ID: 173651458