Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to ?2-microglobulin.
 

Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to ?2-microglobulin.

http://www.bionmr.com//www.ncbi.nlm....PubMedLink.gif http://www.bionmr.com//www.ncbi.nlm....elsevieroa.png Related Articles Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to ?2-microglobulin.

Biochim Biophys Acta Proteins Proteom. 2020 Dec 23;:140593

Authors: Yoshimura Y, So M, Miyanoiri Y

Abstract
The 15N1H heteronuclear single-quantum correlation (HSQC) technique in protein NMR spectroscopy suffers from line-broadening effects, such as chemical exchange of labile protons with solvent, and exchange broadening for residues undergoing conformational dynamics. The amide resonance of ?2-microglobulin residue S88 is not observed in the HSQC spectrum but can be obtained through 13C-detect experiments that circumvent the problem of amide-solvent exchange broadening. Line broadening of S88 resonance beyond detection in the HSQC spectrum is not attributed to conformational exchange but rather to solvent exchange occurring on the order of ~103 s-1.


PMID: 33359410 [PubMed - as supplied by publisher]



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