Sequential individual resonance assignments in the ¹H‐NMR spectra of polypeptides and proteins

Abstract

Abstract Recently, a new procedure for the assignment of protein 1 H‐nmr spectra was introduced that relies on stereochemical considerations of proton–proton distances in polypeptides and on the use of two‐dimensional nmr for obtaining 1 H‐ 1 H through‐bond and through‐space connectivity maps. In the present paper a particular aspect of this assignment procedure is discussed in more detail, i.e., how to obtain individual resonance assignments from identification of amino acid side‐chain spin systems and identification of neighboring residues in the amino acid sequence.