ARCHE-NOAH: NMR supersequence with five different CEST experiments for studying protein conformational dynamics

Rodrigo Cabrera Allpas; Alexandar L Hansen; Rafael Brüschweiler

doi:10.1039/d3cp01580g

ARCHE-NOAH: NMR supersequence with five different CEST experiments for studying protein conformational dynamics

Phys Chem Chem Phys. 2023 Jun 21;25(24):16217-16221. doi: 10.1039/d3cp01580g.

Authors

Rodrigo Cabrera Allpas¹, Alexandar L Hansen², Rafael Brüschweiler^{1

2

3}

Affiliations

¹ Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA. bruschweiler.1@osu.edu.
² Campus Chemical Instrument Center, The Ohio State University, Columbus, Ohio 43210, USA.
³ Department of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, Ohio 43210, USA.

PMID: 37288747
DOI: 10.1039/d3cp01580g

Abstract

An NMR NOAH-supersequence is presented consisting of five CEST experiments for studying protein backbone and side-chain dynamics by ¹⁵N-CEST, carbonyl-¹³CO-CEST, aromatic-¹³C_ar-CEST, ¹³C_α-CEST, and methyl-¹³C_met-CEST. The new sequence acquires the data for these experiments in a fraction of the time required for the individual experiments, saving over four days of NMR time per sample.

MeSH terms

Magnetic Resonance Imaging*
Magnetic Resonance Spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Proteins* / chemistry

Substances

Proteins