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Protein deuteration via algal amino acids to circumvent proton back-exchange for ¹H-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 via algal amino acids to circumvent proton back-exchange for 1H-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 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. ...[more]

PMID: 38407363

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