Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics
<p>The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular, irreversible foldi...
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doaj-70b11156150e4eab8d727ecc445982ab2021-08-02T22:20:19ZengCopernicus PublicationsMagnetic Resonance2699-00162021-05-01229132010.5194/mr-2-291-2021Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamicsG. Pintér0K. F. Hohmann1J. T. Grün2J. Wirmer-Bartoschek3C. Glaubitz4B. Fürtig5H. Schwalbe6Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Biophysical Chemistry, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, GermanyInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, Germany<p>The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular, irreversible folding experiments pose large requirements for (i) signal-to-noise due to the time limitations and (ii) synchronising of the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the study of time-resolved NMR studies. Further, methods are reviewed ranging from pressure and temperature jump, light induction to rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.</p>https://mr.copernicus.org/articles/2/291/2021/mr-2-291-2021.pdf |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
G. Pintér K. F. Hohmann J. T. Grün J. Wirmer-Bartoschek C. Glaubitz B. Fürtig H. Schwalbe |
spellingShingle |
G. Pintér K. F. Hohmann J. T. Grün J. Wirmer-Bartoschek C. Glaubitz B. Fürtig H. Schwalbe Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics Magnetic Resonance |
author_facet |
G. Pintér K. F. Hohmann J. T. Grün J. Wirmer-Bartoschek C. Glaubitz B. Fürtig H. Schwalbe |
author_sort |
G. Pintér |
title |
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
title_short |
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
title_full |
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
title_fullStr |
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
title_full_unstemmed |
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
title_sort |
real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics |
publisher |
Copernicus Publications |
series |
Magnetic Resonance |
issn |
2699-0016 |
publishDate |
2021-05-01 |
description |
<p>The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and
DNA. Time-resolved NMR experiments can be conducted in a reversible or an
irreversible manner. In particular, irreversible folding experiments pose large requirements for (i) signal-to-noise due to the time limitations
and (ii) synchronising of the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the
study of time-resolved NMR studies. Further, methods are reviewed ranging
from pressure and temperature jump, light induction to rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.</p> |
url |
https://mr.copernicus.org/articles/2/291/2021/mr-2-291-2021.pdf |
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