Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding. J Biomol NMR 2025 Mar;79(1):35-45
Date
01/30/2025Pubmed ID
39881117Pubmed Central ID
PMC12500234DOI
10.1007/s10858-024-00455-6Scopus ID
2-s2.0-85217365606 (requires institutional sign-in at Scopus site) 1 CitationAbstract
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and hydrogen exchange. In this work, we demonstrate a protocol for multi-dimensional solid-state NMR spectral editing of signals from basic sidechains based on Hadamard matrix encoding. The Hadamard method acquires multi-dimensional experiments in such a way that both the backbone and under-sampled sidechain signals can be decoded for unambiguous editing in the 15N spectral frequency dimension. All multi-dimensional 15N-edited solid-state NMR experiments can be acquired using this strategy, thereby accelerating the acquisition of spectra spanning broad frequency bandwidth. Application of these methods to the ferritin nanocage, reveals signals from N atoms from His, Arg, Lys and Trp sidechains, as well as their tightly bound, ordered water molecules. The Hadamard approach adds to the arsenal of spectroscopic approaches for protein NMR signal detection.
Author List
Gopinath T, Kraft A, Shin K, Wood NA, Marassi FMAuthors
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinKyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
Gopinath Tata PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
Nicholas A. Wood Postdoctoral Researcher 2 in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
ArginineFerritins
Histidine
Lysine
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Proteins
