Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR. Issue 12 (21st December 2015)

• Record Type: Journal Article
• Authors: Vasa, Suresh Kumar; Rovó, Petra; Giller, Karin; Becker, Stefan; Linser, Rasmus
• Is Part Of: Physical chemistry chemical physics. Volume 18:Issue 12(2016)
• Page Start: 8359
• Page End: 8363
• Publication Date: 2015-12-21
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.3
• DOI: 10.1039/c5cp06601h
• Languages: English
• ISSNs: 1463-9076

Abstract

Abstract : Aliphatic protons as reporters: aliphatic protons are abundant nuclei in biopolymers and rich in spectroscopic, chemical, and biophysical information. Readout of individual proton chemical shifts with a backbone amide resolution via iSOCP enables facilitated access to this information content despite minimal protein amounts without deuteration. Abstract : Interactions within proteins, with their surrounding, and with other molecules are mediated mostly by hydrogen atoms. In fully protonated, inhomogeneous, or larger proteins, however, aliphatic proton shifts tend to show little dispersion despite fast Magic-Angle Spinning. 3D correlations dispersing aliphatic proton shifts by their better resolved amide N/H shifts can alleviate this problem. Using inverse second-order cross-polarization (iSOCP), we here introduce dedicated and improved means to sensitively link site-specific chemical shift information from aliphatic protons with a backbone amide resolution. Thus, even in cases where protein deuteration is impossible, this approach may enable access to various aspects of protein functions that are reported on by protons.