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核心技术专利：CN118964589B侵权必究
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用于生物分子动力学研究的实时核磁共振光谱学。

Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.

作者信息

Pintér György, Hohmann Katharina F, Grün J Tassilo, Wirmer-Bartoschek Julia, Glaubitz Clemens, Fürtig Boris, Schwalbe Harald

机构信息

Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, Germany.

Institute for Biophysical Chemistry, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt 60438, Germany.

出版信息

Magn Reson (Gott). 2021 May 11;2(1):291-320. doi: 10.5194/mr-2-291-2021. eCollection 2021.

DOI:10.5194/mr-2-291-2021
PMID:37904763
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10539803/
Abstract

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.

摘要

这篇综述描述了核磁共振（NMR）光谱法在研究蛋白质、RNA和DNA的折叠、重折叠及聚集动力学方面的应用。时间分辨核磁共振实验可以可逆或不可逆的方式进行。特别是，不可逆折叠实验对（i）由于时间限制导致的信噪比以及（ii）重折叠步骤的同步提出了很高的要求。因此，本文讨论了提高信噪比的方法的应用，包括动态核极化、超极化和光化学诱导动态核极化，用于时间分辨核磁共振研究。此外，还综述了从压力和温度跃变、光诱导到快速混合等方法，以诱导启动折叠所需的快速非平衡条件。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/164db1973eb0/mr-2-291-f15.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/4031eca0268e/mr-2-291-f01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/71889268f36f/mr-2-291-f02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/8bc78e57d79e/mr-2-291-f03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/62338910ce90/mr-2-291-f04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/9a318c441cb9/mr-2-291-f05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/4e201cc2a69e/mr-2-291-f06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/710ea37c299d/mr-2-291-f07.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/51b34089fb0b/mr-2-291-f08.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/908a35baa49f/mr-2-291-f09.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/c93fc134f5e6/mr-2-291-f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/d32ecaa62664/mr-2-291-f11.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/8f583d5da373/mr-2-291-f12.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/c2a67524d791/mr-2-291-f13.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/1403a6036539/mr-2-291-f14.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/164db1973eb0/mr-2-291-f15.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/4031eca0268e/mr-2-291-f01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/71889268f36f/mr-2-291-f02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/8bc78e57d79e/mr-2-291-f03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/62338910ce90/mr-2-291-f04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/9a318c441cb9/mr-2-291-f05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/4e201cc2a69e/mr-2-291-f06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/710ea37c299d/mr-2-291-f07.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/51b34089fb0b/mr-2-291-f08.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/908a35baa49f/mr-2-291-f09.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/c93fc134f5e6/mr-2-291-f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/d32ecaa62664/mr-2-291-f11.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/8f583d5da373/mr-2-291-f12.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/c2a67524d791/mr-2-291-f13.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/1403a6036539/mr-2-291-f14.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6381/10539803/164db1973eb0/mr-2-291-f15.jpg

相似文献

[1]
Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.

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[2]
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[6]
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[7]
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[8]
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[9]
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本文引用的文献

[1]
Unraveling the Kinetics of Spare-Tire DNA G-Quadruplex Folding.

J Am Chem Soc. 2021-4-28

[2]
Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR.

Sci Adv. 2021-3

[3]
The Folding Landscapes of Human Telomeric RNA and DNA G-Quadruplexes are Markedly Different.

Angew Chem Int Ed Engl. 2021-5-3

[4]
Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.

Nat Commun. 2020-11-4

[5]
DNA mismatches reveal conformational penalties in protein-DNA recognition.

Nature. 2020-11

[6]
Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids.

Nat Commun. 2020-10-21

[7]
Intracellular Binding/Unbinding Kinetics of Approved Drugs to Carbonic Anhydrase II Observed by in-Cell NMR.

ACS Chem Biol. 2020-10-16

[8]
Real-Time In-Cell NMR Reveals the Intracellular Modulation of GTP-Bound Levels of RAS.

Cell Rep. 2020-8-25

[9]
Refolding of Cold-Denatured Barstar Induced by Radio-Frequency Heating: A New Method to Study Protein Folding by Real-Time NMR Spectroscopy.

Angew Chem Int Ed Engl. 2020-12-1

[10]
Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.

Angew Chem Int Ed Engl. 2020-9-1

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