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.

Cold denaturation of the HIV-1 protease monomer / H.I. Rösner, M. Caldarini, A. Prestel, M.A. Vanoni, R.A. Broglia, A. Aliverti, G. Tiana, B.B. Kragelund. - In: BIOCHEMISTRY. - ISSN 0006-2960. - 56:8(2017 Feb 28), pp. 1029-1032. [10.1021/acs.biochem.6b01141]

Cold denaturation of the HIV-1 protease monomer

M. Caldarini
Secondo
;
M.A. Vanoni;A. Aliverti;G. Tiana
Penultimo
;
2017

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.
Settore FIS/03 - Fisica della Materia
28-feb-2017
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/481151
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