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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Biochemistry
Vol/bind	56
Udgave nummer	8
Sider (fra-til)	1029-1032
Antal sider	4
ISSN	0006-2960
DOI	https://doi.org/10.1021/acs.biochem.6b01141
Status	Udgivet - 28 feb. 2017

FN’s Verdensmål

Dette resultat bidrager til følgende verdensmål

Adgang til dokumentet

10.1021/acs.biochem.6b01141

Citationsformater

@article{72a272d577b8435eba65fe48379a08de,

title = "Cold denaturation of the HIV-1 protease monomer",

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.",

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 = "28",

doi = "10.1021/acs.biochem.6b01141",

language = "English",

volume = "56",

pages = "1029--1032",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "8",

}

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 - 2017/2/28

Y1 - 2017/2/28

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.

KW - Journal Article

U2 - 10.1021/acs.biochem.6b01141

DO - 10.1021/acs.biochem.6b01141

M3 - Journal article

C2 - 28168877

SN - 0006-2960

VL - 56

SP - 1029

EP - 1032

JO - Biochemistry

JF - Biochemistry

IS - 8

ER -

Cold denaturation of the HIV-1 protease monomer

Abstract

FN’s Verdensmål

Adgang til dokumentet

Fingeraftryk

Citationsformater