Cold denaturation of the HIV-1 protease monomer

Heike Ilona Rösner; Martina Caldarini; Andreas Prestel; Maria Antonietta Vanoni; Ricardo Americo Broglia; Alessandro Aliverti; Guido Tiana; Birthe Brandt Kragelund

doi:10.1021/acs.biochem.6b01141

Cold denaturation of the HIV-1 protease monomer

Heike Ilona Rösner, Martina Caldarini, Andreas Prestel, Maria Antonietta Vanoni, Ricardo Americo Broglia, Alessandro Aliverti, Guido Tiana, Birthe Brandt Kragelund

2 Citations (Scopus)

Abstract

The human immunodeficiency virus-1 (HIV-1) protease is a complex protein that in its active form adopts a homodimer dominated by β-sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1 protease that is populated above 0 °C and therefore directly accessible to various spectroscopic approaches. Using nuclear magnetic resonance 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 α-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.

Original language	English
Journal	Biochemistry
Volume	56
Issue number	8
Pages (from-to)	1029-1032
Number of pages	4
ISSN	0006-2960
DOIs	https://doi.org/10.1021/acs.biochem.6b01141
Publication status	Published - 28 Feb 2017

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Journal Article

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10.1021/acs.biochem.6b01141

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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 - 2017/2/28

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N2 - The human immunodeficiency virus-1 (HIV-1) protease is a complex protein that in its active form adopts a homodimer dominated by β-sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1 protease that is populated above 0 °C and therefore directly accessible to various spectroscopic approaches. Using nuclear magnetic resonance 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 α-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 human immunodeficiency virus-1 (HIV-1) protease is a complex protein that in its active form adopts a homodimer dominated by β-sheet structures. We have discovered a cold-denatured state of the monomeric subunit of HIV-1 protease that is populated above 0 °C and therefore directly accessible to various spectroscopic approaches. Using nuclear magnetic resonance 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 α-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.

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JO - Biochemistry

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Cold denaturation of the HIV-1 protease monomer

Abstract

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