Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH

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Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH. / Kjærgaard, Magnus; Brander, Søren; Poulsen, Flemming Martin.

I: Journal of Biomolecular N M R, Bind 49, Nr. 2, 02.2011, s. 139-49.

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

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Kjærgaard, Magnus ; Brander, Søren ; Poulsen, Flemming Martin. / Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH. I: Journal of Biomolecular N M R. 2011 ; Bind 49, Nr. 2. s. 139-49.

Bibtex

@article{23a72d1495594cb79310bc41fce7d68f,
title = "Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH",
abstract = "Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970-2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the (13)C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins.",
keywords = "Hydrogen-Ion Concentration, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Proteins, Temperature",
author = "Magnus Kj{\ae}rgaard and S{\o}ren Brander and Poulsen, {Flemming Martin}",
year = "2011",
month = feb,
doi = "10.1007/s10858-011-9472-x",
language = "English",
volume = "49",
pages = "139--49",
journal = "Journal of Biomolecular N M R",
issn = "0925-2738",
publisher = "Springer",
number = "2",

}

RIS

TY - JOUR

T1 - Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH

AU - Kjærgaard, Magnus

AU - Brander, Søren

AU - Poulsen, Flemming Martin

PY - 2011/2

Y1 - 2011/2

N2 - Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970-2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the (13)C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins.

AB - Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970-2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the (13)C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins.

KW - Hydrogen-Ion Concentration

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Folding

KW - Proteins

KW - Temperature

U2 - 10.1007/s10858-011-9472-x

DO - 10.1007/s10858-011-9472-x

M3 - Journal article

C2 - 21234644

VL - 49

SP - 139

EP - 149

JO - Journal of Biomolecular N M R

JF - Journal of Biomolecular N M R

SN - 0925-2738

IS - 2

ER -