Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?
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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 Helene Falsig; Poulsen, Flemming M; Kragelund, Birthe B.
I: Protein Science, Bind 19, Nr. 8, 01.08.2010, s. 1555-64.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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 Helene Falsig
AU - Poulsen, Flemming M
AU - Kragelund, Birthe B
PY - 2010/8/1
Y1 - 2010/8/1
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 -
ID: 33345536