UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates

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• 作者：Maayan Gal ; Paul Schanda ; Bernhard Brutscher ; Lucio Frydman
• 刊名：Journal of the American Chemical Society
• 出版年：2007
• 出版时间：February 7, 2007
• 年：2007
• 卷：129
• 期：5
• 页码：1372 - 1377
• 全文大小：202K
• 年卷期：v.129,no.5(February 7, 2007)
• ISSN：1520-5126

文摘

Following unidirectional biophysical events such as the folding of proteins or the equilibration ofbinding interactions, requires experimental methods that yield information at both atomic-level resolutionand at high repetition rates. Toward this end a number of different approaches enabling the rapid acquisitionof 2D NMR spectra have been recently introduced, including spatially encoded "ultrafast" 2D NMRspectroscopy and SOFAST HMQC NMR. Whereas the former accelerates acquisitions by reducing thenumber of scans that are necessary for completing arbitrary 2D NMR experiments, the latter operates byreducing the delay between consecutive scans while preserving sensitivity. Given the complementaritiesbetween these two approaches it seems natural to combine them into a single tool, enabling the acquisitionof full 2D protein NMR spectra at high repetition rates. We demonstrate here this capability with theintroduction of "ultraSOFAST" HMQC NMR, a spatially encoded and relaxation-optimized approach thatcan provide 2D protein correlation spectra at ~1 s repetition rates for samples in the ~2 mM concentrationrange. The principles, relative advantages, and current limitations of this new approach are discussed,and its application is exemplified with a study of the fast hydrogen-deuterium exchange characterizingamide sites in Ubiquitin.