DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.

Tytuł:: DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.
Autorzy:: Kuwajima K; Department of Physics, School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Yagi-Utsumi M; Exploratory Research Center on Life and Living Systems and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.; Department of Functional Molecular Science, School of Physical Sciences, SOKENDAI (the Graduate University for Advanced Studies), 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.; Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Aichi, Japan.
Yanaka S; Exploratory Research Center on Life and Living Systems and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.; Department of Functional Molecular Science, School of Physical Sciences, SOKENDAI (the Graduate University for Advanced Studies), 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.
Kato K; Exploratory Research Center on Life and Living Systems and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.; Department of Functional Molecular Science, School of Physical Sciences, SOKENDAI (the Graduate University for Advanced Studies), 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Aichi, Japan.; Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Aichi, Japan.
Źródło:: Molecules (Basel, Switzerland) [Molecules] 2022 Jun 10; Vol. 27 (12). Date of Electronic Publication: 2022 Jun 10.
Typ publikacji:: Journal Article; Review
Język:: English
Imprint Name(s):: Original Publication: Basel, Switzerland : MDPI, c1995-
MeSH Terms:: Dimethyl Sulfoxide*/chemistry
Hydrogen*/chemistry
Humans ; Kinetics ; Magnetic Resonance Spectroscopy ; Protein Folding ; Proteins
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Grant Information:: JP20K06574 Japan Society for the Promotion of Science; JPMXP09S21MS0021 Ministry of Education, Culture, Sports, Science and Technology
Contributed Indexing:: Keywords: dimethylsulfoxide; hydrogen/deuterium exchange; nuclear magnetic resonance
Substance Nomenclature:: 0 (Proteins)
7YNJ3PO35Z (Hydrogen)
YOW8V9698H (Dimethyl Sulfoxide)
Entry Date(s):: Date Created: 20220624 Date Completed: 20220627 Latest Revision: 20220716
Update Code:: 20240105
PubMed Central ID:: PMC9230524
DOI:: 10.3390/molecules27123748
PMID:: 35744871
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Pełny tekst

Hydrogen/deuterium (H/D) exchange combined with two-dimensional (2D) NMR spectroscopy has been widely used for studying the structure, stability, and dynamics of proteins. When we apply the H/D-exchange method to investigate non-native states of proteins such as equilibrium and kinetic folding intermediates, H/D-exchange quenching techniques are indispensable, because the exchange reaction is usually too fast to follow by 2D NMR. In this article, we will describe the dimethylsulfoxide (DMSO)-quenched H/D-exchange method and its applications in protein science. In this method, the H/D-exchange buffer is replaced by an aprotic DMSO solution, which quenches the exchange reaction. We have improved the DMSO-quenched method by using spin desalting columns, which are used for medium exchange from the H/D-exchange buffer to the DMSO solution. This improvement has allowed us to monitor the H/D exchange of proteins at a high concentration of salts or denaturants. We describe methodological details of the improved DMSO-quenched method and present a case study using the improved method on the H/D-exchange behavior of unfolded human ubiquitin in 6 M guanidinium chloride.

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