The ¹⁵N–¹H heteronuclear single-quantum correlation (HSQC) technique in protein NMR spectroscopy suffers from line-broadening effects, such as chemical exchange of labile protons with solvent, and exchange broadening for residues undergoing conformational dynamics.

The amide resonance of β₂-microglobulin residue S88 is not observed in the HSQC spectrum but can be obtained through ¹³C-detect experiments that circumvent the problem of amide-solvent exchange broadening.

Line broadening of S88 resonance beyond detection in the HSQC spectrum is not attributed to conformational exchange but rather to solvent exchange occurring on the order of ~10³ s⁻¹.

蛋白质NMR光谱中的¹⁵ N– ¹ H异核单量子相关（HSQC）技术受谱线扩大效应的影响，例如不稳定质子与溶剂的化学交换以及对经历构象动力学的残基进行交换加宽。

β的酰胺共振₂ -微球蛋白残基S88没有在HSQC光谱中观察到，但可以通过获得¹³ C-检测实验规避酰胺溶剂交换变宽的问题。

S88共振的线展宽超出了HSQC光谱中的检测范围，这不归因于构象交换，而是归因于约10 ³  s ^-1的溶剂交换。