Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00126458" target="_blank" >RIV/00216224:14740/22:00126458 - isvavai.cz</a>
Result on the web
<a href="https://www.science.org/doi/10.1126/sciadv.abq5179" target="_blank" >https://www.science.org/doi/10.1126/sciadv.abq5179</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1126/sciadv.abq5179" target="_blank" >10.1126/sciadv.abq5179</a>
Alternative languages
Result language
angličtina
Original language name
Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces
Original language description
Nuclear magnetic resonance (NMR) spectroscopy is a key method for determining the structural dynamics of proteins in their native solution state. However, the low sensitivity of NMR typically necessitates nonphysiologically high sample concentrations, which often limit the relevance of the recorded data. We show how to use hyperpolarized water by dissolution dynamic nuclear polarization (DDNP) to acquire protein spectra at concentrations of 1.M within seconds and with a high signal-to-noise ratio. The importance of approaching physiological concentrations is demonstrated for the vital MYC-associated factor X, which we show to switch conformations when diluted. While in vitro conditions lead to a population of the well-documented dimer, concentrations lowered by more than two orders of magnitude entail dimer dissociation and formation of a globularly folded monomer. We identified this structure by integrating DDNP with computational techniques to overcome the often-encountered constraint of DDNP of limited structural information provided by the typically detected one-dimensional spectra.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Science advances
ISSN
2375-2548
e-ISSN
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Volume of the periodical
8
Issue of the periodical within the volume
31
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
1-7
UT code for WoS article
000836990600040
EID of the result in the Scopus database
2-s2.0-85135462122