Anal Chem. 2012 Jan 17;84(2):867-70. doi: 10.1021/ac202818m. Epub 2011 Dec 23.
A combination of chemical cross-linking and hydrogen-deuterium exchange coupled to high resolution mass spectrometry was used to describe structural differences of NKR-P1A receptor. The loop region extended from the compact core in the crystal structure was found to be closely attached to the protein core in solution. Our approach has potential to refine protein structures in solution within a few days and has very low sample consumption.
采用化学交联和氢氘交换结合高分辨质谱的方法来描述 NKRP1A 受体的结构差异。晶体结构中从紧凑核心延伸出的环区在溶液中被发现紧密附着在蛋白质核心上。我们的方法具有在几天内精修溶液中蛋白质结构的潜力，并且样品消耗量非常低。
