Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?

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Standard

Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? / Kjærgaard, Magnus; Nørholm, Ann-Beth; Hendus-Altenburger, Ruth; Pedersen, Stine F; Poulsen, Flemming Martin; Kragelund, Birthe Brandt.

I: Protein Science, Bind 19, Nr. 8, 08.2010, s. 1555-64.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Kjærgaard, M, Nørholm, A-B, Hendus-Altenburger, R, Pedersen, SF, Poulsen, FM & Kragelund, BB 2010, 'Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?', Protein Science, bind 19, nr. 8, s. 1555-64. https://doi.org/10.1002/pro.435

APA

Kjærgaard, M., Nørholm, A-B., Hendus-Altenburger, R., Pedersen, S. F., Poulsen, F. M., & Kragelund, B. B. (2010). Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? Protein Science, 19(8), 1555-64. https://doi.org/10.1002/pro.435

CBE

Kjærgaard M, Nørholm A-B, Hendus-Altenburger R, Pedersen SF, Poulsen FM, Kragelund BB. 2010. Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?. Protein Science. 19(8):1555-64. https://doi.org/10.1002/pro.435

MLA

Vancouver

Kjærgaard M, Nørholm A-B, Hendus-Altenburger R, Pedersen SF, Poulsen FM, Kragelund BB. Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? Protein Science. 2010 aug;19(8):1555-64. https://doi.org/10.1002/pro.435

Author

Kjærgaard, Magnus ; Nørholm, Ann-Beth ; Hendus-Altenburger, Ruth ; Pedersen, Stine F ; Poulsen, Flemming Martin ; Kragelund, Birthe Brandt. / Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?. I: Protein Science. 2010 ; Bind 19, Nr. 8. s. 1555-64.

Bibtex

@article{ae4a476877814fffa2ef7495c31ca41e,
title = "Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?",
abstract = "Structural characterization of intrinsically disordered proteins (IDPs) is mandatory for deciphering their potential unique physical and biological properties. A large number of circular dichroism (CD) studies have demonstrated that a structural change takes place in IDPs with increasing temperature, which most likely reflects formation of transient alpha-helices or loss of polyproline II (PPII) content. Using three IDPs, ACTR, NHE1, and Spd1, we show that the temperature-induced structural change is common among IDPs and is accompanied by a contraction of the conformational ensemble. This phenomenon was explored at residue resolution by multidimensional NMR spectroscopy. Intrinsic chemical shift referencing allowed us to identify regions of transiently formed helices and their temperature-dependent changes in helicity. All helical regions were found to lose rather than gain helical structures with increasing temperature, and accordingly these were not responsible for the change in the CD spectra. In contrast, the nonhelical regions exhibited a general temperature-dependent structural change that was independent of long-range interactions. The temperature-dependent CD spectroscopic signature of IDPs that has been amply documented can be rationalized to represent redistribution of the statistical coil involving a general loss of PPII conformations.",
keywords = "Cation Transport Proteins, Circular Dichroism, Fungal Proteins, Humans, Nuclear Magnetic Resonance, Biomolecular, Peptides, Protein Structure, Secondary, Scattering, Small Angle, Sodium-Hydrogen Antiporter, Temperature",
author = "Magnus Kj{\ae}rgaard and Ann-Beth N{\o}rholm and Ruth Hendus-Altenburger and Pedersen, {Stine F} and Poulsen, {Flemming Martin} and Kragelund, {Birthe Brandt}",
year = "2010",
month = aug,
doi = "10.1002/pro.435",
language = "English",
volume = "19",
pages = "1555--64",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell Publishing, Inc.",
number = "8",

}

RIS

TY - JOUR

T1 - Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?

AU - Kjærgaard, Magnus

AU - Nørholm, Ann-Beth

AU - Hendus-Altenburger, Ruth

AU - Pedersen, Stine F

AU - Poulsen, Flemming Martin

AU - Kragelund, Birthe Brandt

PY - 2010/8

Y1 - 2010/8

N2 - Structural characterization of intrinsically disordered proteins (IDPs) is mandatory for deciphering their potential unique physical and biological properties. A large number of circular dichroism (CD) studies have demonstrated that a structural change takes place in IDPs with increasing temperature, which most likely reflects formation of transient alpha-helices or loss of polyproline II (PPII) content. Using three IDPs, ACTR, NHE1, and Spd1, we show that the temperature-induced structural change is common among IDPs and is accompanied by a contraction of the conformational ensemble. This phenomenon was explored at residue resolution by multidimensional NMR spectroscopy. Intrinsic chemical shift referencing allowed us to identify regions of transiently formed helices and their temperature-dependent changes in helicity. All helical regions were found to lose rather than gain helical structures with increasing temperature, and accordingly these were not responsible for the change in the CD spectra. In contrast, the nonhelical regions exhibited a general temperature-dependent structural change that was independent of long-range interactions. The temperature-dependent CD spectroscopic signature of IDPs that has been amply documented can be rationalized to represent redistribution of the statistical coil involving a general loss of PPII conformations.

AB - Structural characterization of intrinsically disordered proteins (IDPs) is mandatory for deciphering their potential unique physical and biological properties. A large number of circular dichroism (CD) studies have demonstrated that a structural change takes place in IDPs with increasing temperature, which most likely reflects formation of transient alpha-helices or loss of polyproline II (PPII) content. Using three IDPs, ACTR, NHE1, and Spd1, we show that the temperature-induced structural change is common among IDPs and is accompanied by a contraction of the conformational ensemble. This phenomenon was explored at residue resolution by multidimensional NMR spectroscopy. Intrinsic chemical shift referencing allowed us to identify regions of transiently formed helices and their temperature-dependent changes in helicity. All helical regions were found to lose rather than gain helical structures with increasing temperature, and accordingly these were not responsible for the change in the CD spectra. In contrast, the nonhelical regions exhibited a general temperature-dependent structural change that was independent of long-range interactions. The temperature-dependent CD spectroscopic signature of IDPs that has been amply documented can be rationalized to represent redistribution of the statistical coil involving a general loss of PPII conformations.

KW - Cation Transport Proteins

KW - Circular Dichroism

KW - Fungal Proteins

KW - Humans

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Peptides

KW - Protein Structure, Secondary

KW - Scattering, Small Angle

KW - Sodium-Hydrogen Antiporter

KW - Temperature

U2 - 10.1002/pro.435

DO - 10.1002/pro.435

M3 - Journal article

C2 - 20556825

VL - 19

SP - 1555

EP - 1564

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 8

ER -