Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems

Aneta J. Lenard; Frans A.A. Mulder; Tobias Madl

doi:10.1016/j.pnmrs.2022.09.001

Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems

Aneta J. Lenard, Frans A.A. Mulder, Tobias Madl^*

^*Corresponding author for this work

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

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Abstract

Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic resonance (NMR)-based method that allows characterization of the structure and dynamics of biomolecular systems through providing quantitative experimental information on solvent accessibility of NMR-active nuclei. Addition of soluble paramagnetic probes to the solution of a biomolecule leads to paramagnetic relaxation enhancement in a concentration-dependent manner. Here we review recent progress in the sPRE-based characterization of structural and dynamic properties of biomolecules and their complexes, and aim to deliver a comprehensive illustration of a growing number of applications of the method to various biological systems. We discuss the physical principles of sPRE measurements and provide an overview of available co-solute paramagnetic probes. We then explore how sPRE, in combination with complementary biophysical techniques, can further advance biomolecular structure determination, identification of interaction surfaces within protein complexes, and probing of conformational changes and low-population transient states, as well as deliver insights into weak, nonspecific, and transient interactions between proteins and co-solutes. In addition, we present examples of how the incorporation of solvent paramagnetic probes can improve the sensitivity of NMR experiments and discuss the prospects of applying sPRE to NMR metabolomics, drug discovery, and the study of intrinsically disordered proteins.

Original language	English
Journal	Progress in Nuclear Magnetic Resonance Spectroscopy
Volume	132-133
Pages (from-to)	113-139
Number of pages	27
ISSN	0079-6565
DOIs	https://doi.org/10.1016/j.pnmrs.2022.09.001
Publication status	Published - Oct 2022

Keywords

Nuclear magnetic resonance (NMR) spectroscopy
Paramagnetic co-solutes
Solvent accessibility
Solvent paramagnetic relaxation enhancement (sPRE)
Structural biology
Magnetic Resonance Spectroscopy
Solutions
Intrinsically Disordered Proteins/chemistry
Nuclear Magnetic Resonance, Biomolecular/methods
Solvents/chemistry

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1-s2.0-S0079656522000243-mainFinal published version, 3.34 MBLicence: CC BY

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title = "Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems",

abstract = "Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic resonance (NMR)-based method that allows characterization of the structure and dynamics of biomolecular systems through providing quantitative experimental information on solvent accessibility of NMR-active nuclei. Addition of soluble paramagnetic probes to the solution of a biomolecule leads to paramagnetic relaxation enhancement in a concentration-dependent manner. Here we review recent progress in the sPRE-based characterization of structural and dynamic properties of biomolecules and their complexes, and aim to deliver a comprehensive illustration of a growing number of applications of the method to various biological systems. We discuss the physical principles of sPRE measurements and provide an overview of available co-solute paramagnetic probes. We then explore how sPRE, in combination with complementary biophysical techniques, can further advance biomolecular structure determination, identification of interaction surfaces within protein complexes, and probing of conformational changes and low-population transient states, as well as deliver insights into weak, nonspecific, and transient interactions between proteins and co-solutes. In addition, we present examples of how the incorporation of solvent paramagnetic probes can improve the sensitivity of NMR experiments and discuss the prospects of applying sPRE to NMR metabolomics, drug discovery, and the study of intrinsically disordered proteins.",

keywords = "Nuclear magnetic resonance (NMR) spectroscopy, Paramagnetic co-solutes, Solvent accessibility, Solvent paramagnetic relaxation enhancement (sPRE), Structural biology, Magnetic Resonance Spectroscopy, Solutions, Intrinsically Disordered Proteins/chemistry, Nuclear Magnetic Resonance, Biomolecular/methods, Solvents/chemistry",

author = "Lenard, {Aneta J.} and Mulder, {Frans A.A.} and Tobias Madl",

year = "2022",

month = oct,

doi = "10.1016/j.pnmrs.2022.09.001",

language = "English",

volume = "132-133",

pages = "113--139",

journal = "Progress in Nuclear Magnetic Resonance Spectroscopy",

issn = "0079-6565",

publisher = "Elsevier B.V.",

}

Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems. / Lenard, Aneta J.; Mulder, Frans A.A.; Madl, Tobias.
In: Progress in Nuclear Magnetic Resonance Spectroscopy, Vol. 132-133, 10.2022, p. 113-139.

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

TY - JOUR

T1 - Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems

AU - Lenard, Aneta J.

AU - Mulder, Frans A.A.

AU - Madl, Tobias

PY - 2022/10

Y1 - 2022/10

N2 - Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic resonance (NMR)-based method that allows characterization of the structure and dynamics of biomolecular systems through providing quantitative experimental information on solvent accessibility of NMR-active nuclei. Addition of soluble paramagnetic probes to the solution of a biomolecule leads to paramagnetic relaxation enhancement in a concentration-dependent manner. Here we review recent progress in the sPRE-based characterization of structural and dynamic properties of biomolecules and their complexes, and aim to deliver a comprehensive illustration of a growing number of applications of the method to various biological systems. We discuss the physical principles of sPRE measurements and provide an overview of available co-solute paramagnetic probes. We then explore how sPRE, in combination with complementary biophysical techniques, can further advance biomolecular structure determination, identification of interaction surfaces within protein complexes, and probing of conformational changes and low-population transient states, as well as deliver insights into weak, nonspecific, and transient interactions between proteins and co-solutes. In addition, we present examples of how the incorporation of solvent paramagnetic probes can improve the sensitivity of NMR experiments and discuss the prospects of applying sPRE to NMR metabolomics, drug discovery, and the study of intrinsically disordered proteins.

AB - Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic resonance (NMR)-based method that allows characterization of the structure and dynamics of biomolecular systems through providing quantitative experimental information on solvent accessibility of NMR-active nuclei. Addition of soluble paramagnetic probes to the solution of a biomolecule leads to paramagnetic relaxation enhancement in a concentration-dependent manner. Here we review recent progress in the sPRE-based characterization of structural and dynamic properties of biomolecules and their complexes, and aim to deliver a comprehensive illustration of a growing number of applications of the method to various biological systems. We discuss the physical principles of sPRE measurements and provide an overview of available co-solute paramagnetic probes. We then explore how sPRE, in combination with complementary biophysical techniques, can further advance biomolecular structure determination, identification of interaction surfaces within protein complexes, and probing of conformational changes and low-population transient states, as well as deliver insights into weak, nonspecific, and transient interactions between proteins and co-solutes. In addition, we present examples of how the incorporation of solvent paramagnetic probes can improve the sensitivity of NMR experiments and discuss the prospects of applying sPRE to NMR metabolomics, drug discovery, and the study of intrinsically disordered proteins.

KW - Nuclear magnetic resonance (NMR) spectroscopy

KW - Paramagnetic co-solutes

KW - Solvent accessibility

KW - Solvent paramagnetic relaxation enhancement (sPRE)

KW - Structural biology

KW - Magnetic Resonance Spectroscopy

KW - Solutions

KW - Intrinsically Disordered Proteins/chemistry

KW - Nuclear Magnetic Resonance, Biomolecular/methods

KW - Solvents/chemistry

U2 - 10.1016/j.pnmrs.2022.09.001

DO - 10.1016/j.pnmrs.2022.09.001

M3 - Journal article

C2 - 36496256

SN - 0079-6565

VL - 132-133

SP - 113

EP - 139

JO - Progress in Nuclear Magnetic Resonance Spectroscopy

JF - Progress in Nuclear Magnetic Resonance Spectroscopy

ER -

Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems

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Keywords

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