Rao Kakita Veera Mohana, Bopardikar Mandar, Kumar Shukla Vaibhav, Rachineni Kavitha, Ranjan Priyatosh, Singh Jai Shankar, Hosur Ramakrishna V
UM-DAE Centre for Excellence in Basic Sciences, University of Mumbai Kalina Campus, Santacruz Mumbai 400 098 India.
Department of Chemical Sciences, Tata Institute of Fundamental Research (TIFR) 1-Homi Bhabha Road, Colaba Mumbai 400 005 India
RSC Adv. 2018 May 15;8(32):17616-17621. doi: 10.1039/c8ra00527c. eCollection 2018 May 14.
Application of Non Uniform Sampling (NUS) along with Band-selective Excitation Short-Transient (BEST) NMR experiments has been demonstrated for obtaining the important residue-specific atomic level backbone chemical shift values in short durations of time. This application has been demonstrated with both well-folded (ubiquitin) and unfolded (α-synuclein) proteins alike. With this strategy, the experiments required for determining backbone chemical shifts can be performed very rapidly, , in ∼2 hours of spectrometer time, and this data can be used to calculate the backbone folds of proteins using well established algorithms. This will be of great value for structural proteomic investigations on one hand, where the speed of structure determination is a limiting factor and for application in the study of slow kinetic processes involving proteins, such as fibrillization, on the other hand.
非均匀采样（NUS）与带选择激发短瞬态（BEST）核磁共振实验相结合，已被证明可在短时间内获得重要的、特定残基的原子水平主链化学位移值。这种应用已在折叠良好的（泛素）和未折叠的（α-突触核蛋白）蛋白质中得到证实。采用这种策略，确定主链化学位移所需的实验可以非常迅速地完成，大约只需2小时的光谱仪时间，并且这些数据可用于使用成熟的算法计算蛋白质的主链折叠。一方面，这对于结构蛋白质组学研究具有重要价值，因为结构测定的速度是一个限制因素；另一方面，对于涉及蛋白质的缓慢动力学过程（如纤维化）的研究应用也具有重要价值。
