Clean SEA-TROSY Experiments to Map Solvent Exposed Amides in Large Proteins

• 来源期刊: 中国化学（英文版）
• 年，卷（期）: 2004,（12）
• 页码范围: 1395-1398
• 页数: 4页
• 语种: 英文

摘要

It is well known that the SEA-TROSY experiment could alleviate some of the problems of resonance overlap in 15N/2H labeled proteins as it was designed to selectively map solvent exposed amide protons. However, SEATROSY 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.