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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Copernicus Publications
2021-05-01
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| Series: | Magnetic Resonance |
| Online Access: | https://mr.copernicus.org/articles/2/291/2021/mr-2-291-2021.pdf |
| _version_ | 1818690367891963904 |
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| author | G. Pintér K. F. Hohmann J. T. Grün J. Wirmer-Bartoschek C. Glaubitz B. Fürtig H. Schwalbe |
| author_facet | G. Pintér K. F. Hohmann J. T. Grün J. Wirmer-Bartoschek C. Glaubitz B. Fürtig H. Schwalbe |
| author_sort | G. Pintér |
| collection | DOAJ |
| 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> |
| first_indexed | 2024-12-17T12:24:53Z |
| format | Article |
| id | doaj.art-70b11156150e4eab8d727ecc445982ab |
| institution | Directory Open Access Journal |
| issn | 2699-0016 |
| language | English |
| last_indexed | 2024-12-17T12:24:53Z |
| publishDate | 2021-05-01 |
| publisher | Copernicus Publications |
| record_format | Article |
| series | Magnetic Resonance |
| spelling | doaj.art-70b11156150e4eab8d727ecc445982ab2022-12-21T21:48:49ZengCopernicus 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 |
| 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 |
| title | 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_short | 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 |
| url | https://mr.copernicus.org/articles/2/291/2021/mr-2-291-2021.pdf |
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