Super-resolution triple-resonance NMR spectroscopy for the sequential assignment of proteins.

Authors

Olivia Gampp, Luca Wenchel, Peter Güntert, Piotr Klukowski, Roland Riek

Published in

Science advances. Volume 11. Issue 33. Pages eadv6246. Aug 15, 2025. Epub Aug 15, 2025.

Abstract

To study the structure and dynamics of proteins by nuclear magnetic resonance (NMR), sequence-specific assignment is needed, which can be obtained by acquiring and analyzing multiple triple-resonance experiments with the three-dimensional TROSY-HNCA, the most sensitive stand-alone experiment with which sequential assignment is, in principle, possible. However, gaining an unambiguous assignment solely from this spectrum is generally not possible because amino acid-type information cannot be gleaned only from the ¹³C^α shifts and the low resolution in the ¹³C dimension, which is limited by the homonuclear coupling of the ¹³C^α and ¹³C^β nuclei. Here, super-resolution NMR is applied to the TROSY-HNCA and HNcoCA experiments, yielding pseudo-decoupling, which results in a four- to fivefold resolution enhancement in the ¹³C dimension, essential for the assignment, which allows for straightforward assignment of proteins as large as 500 residues based on simulations.

PMID:
40815649
Bibliographic data and abstract were imported from PubMed on 16 Aug 2025.

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