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Protein deuteration <i>via</i> algal amino acids to circumvent proton back-exchange for <sup>1</sup>H-detected solid-state NMR.

ABSTRACT: With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies.

SUBMITTER: Aucharova H 

PROVIDER: S-EPMC10928984 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

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Protein deuteration &lt;i&gt;via&lt;/i&gt; algal amino acids to circumvent proton back-exchange for &lt;sup&gt;1&lt;/sup&gt;H-detected solid-state NMR.

Aucharova Hanna H   Klein Alexander A   Gomez Sara Medina SM   Söldner Benedikt B   Vasa Suresh K SK   Linser Rasmus R  

Chemical communications (Cambridge, England) 20240312 22

With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively <i>via</i> deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies. ...[more]

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