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Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses

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Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. / Kjærgaard, Magnus; Poulsen, Flemming Martin; Kragelund, Birthe Brandt.

In: Methods in molecular biology (Clifton, N.J.), Vol. 896, 2012, p. 249-56.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Kjærgaard, M, Poulsen, FM & Kragelund, BB 2012, 'Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses', Methods in molecular biology (Clifton, N.J.), vol. 896, pp. 249-56. https://doi.org/10.1007/978-1-4614-3704-8_16

APA

Kjærgaard, M., Poulsen, F. M., & Kragelund, B. B. (2012). Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. Methods in molecular biology (Clifton, N.J.), 896, 249-56. https://doi.org/10.1007/978-1-4614-3704-8_16

CBE

Kjærgaard M, Poulsen FM, Kragelund BB. 2012. Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. Methods in molecular biology (Clifton, N.J.). 896:249-56. https://doi.org/10.1007/978-1-4614-3704-8_16

MLA

Kjærgaard, Magnus, Flemming Martin Poulsen and Birthe Brandt Kragelund. "Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses". Methods in molecular biology (Clifton, N.J.). 2012, 896. 249-56. https://doi.org/10.1007/978-1-4614-3704-8_16

Vancouver

Kjærgaard M, Poulsen FM, Kragelund BB. Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. Methods in molecular biology (Clifton, N.J.). 2012;896:249-56. doi: 10.1007/978-1-4614-3704-8_16

Author

Kjærgaard, Magnus ; Poulsen, Flemming Martin ; Kragelund, Birthe Brandt. / Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. In: Methods in molecular biology (Clifton, N.J.). 2012 ; Vol. 896. pp. 249-56.

Bibtex

@article{225db0e2c8bd40de9815fd1c12558b8c,
title = "Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses",
abstract = "Intrinsically disordered proteins are abundant in nature and perform many important physiological functions. Multidimensional NMR spectroscopy has been crucial for the understanding of the conformational properties of disordered proteins and is increasingly used to probe their conformational ensembles. Compared to folded proteins, disordered proteins are more malleable and more easily perturbed by environmental factors. Accordingly, the experimental conditions and especially the temperature modify the structural and functional properties of disordered proteins. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins using chemical shifts.",
keywords = "Analytic Sample Preparation Methods, Calibration, Nuclear Magnetic Resonance, Biomolecular, Proteins, Temperature",
author = "Magnus Kj{\ae}rgaard and Poulsen, {Flemming Martin} and Kragelund, {Birthe Brandt}",
year = "2012",
doi = "10.1007/978-1-4614-3704-8_16",
language = "English",
volume = "896",
pages = "249--56",
journal = "Methods in Molecular Biology",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses

AU - Kjærgaard, Magnus

AU - Poulsen, Flemming Martin

AU - Kragelund, Birthe Brandt

PY - 2012

Y1 - 2012

N2 - Intrinsically disordered proteins are abundant in nature and perform many important physiological functions. Multidimensional NMR spectroscopy has been crucial for the understanding of the conformational properties of disordered proteins and is increasingly used to probe their conformational ensembles. Compared to folded proteins, disordered proteins are more malleable and more easily perturbed by environmental factors. Accordingly, the experimental conditions and especially the temperature modify the structural and functional properties of disordered proteins. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins using chemical shifts.

AB - Intrinsically disordered proteins are abundant in nature and perform many important physiological functions. Multidimensional NMR spectroscopy has been crucial for the understanding of the conformational properties of disordered proteins and is increasingly used to probe their conformational ensembles. Compared to folded proteins, disordered proteins are more malleable and more easily perturbed by environmental factors. Accordingly, the experimental conditions and especially the temperature modify the structural and functional properties of disordered proteins. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins using chemical shifts.

KW - Analytic Sample Preparation Methods

KW - Calibration

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Proteins

KW - Temperature

U2 - 10.1007/978-1-4614-3704-8_16

DO - 10.1007/978-1-4614-3704-8_16

M3 - Journal article

C2 - 22821529

VL - 896

SP - 249

EP - 256

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -