Premium
Clean SEA‐TROW experiments to map solvent exposed amides in large proteins
Author(s) -
Lin DongHai
Publication year - 2004
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20040221203
Subject(s) - chemistry , protonation , deuterium , amide , solvent , amine gas treating , relaxation (psychology) , molecule , organic chemistry , atomic physics , ion , social psychology , psychology , physics
It is well known that the SEA‐TROSY experiment could alleviate some of the problems of resonance overlap in 15 N/ 2 H labeled proteins as it was designed to selectively map solvent exposed amide protons. However, SEA‐TROSY spectra may be contaminated with exchange‐relayed NOE contributions from fast exchanged hydroxyl or amine protons and contributions from longitudinal relaxation. Also, perdeuteration of the protein sample is a prerequisite for this experiment. In this communication, a modified version, clean SEA‐TROSY, was proposed to eliminate these artifacts and to allow the experiment to be applied to protonated or partially deuterated proteins and protein complexes.