The exchange of molecules between different physical or chemical environments due to diffusion or chemical transformations has a crucial role in a plethora of fundamental processes such as breathing, protein folding, chemical reactions and catalysis. Here, we introduce a method for a single-scan, ultrafast NMR analysis of molecular exchange based on the diffusion coefficient contrast. The method shortens the experiment time by one to four orders of magnitude. Consequently, it opens the way for high sensitivity quantification of important transient physical and chemical exchange processes such as in cellular metabolism. As a proof of principle, we demonstrate that the method reveals the structure of aggregates formed by surfactants relevant to aerosol research.

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Molecular exchange processes are ubiquitous in nature. Here, we introduce a method to analyze exchange processes by using low-cost, portable, singlesided NMR instruments. The inherent magnetic field inhomogeneity of the single-sided instruments is exploited to achieve diffusion contrast of exchange sites and spatial encoding of 2D data. This so-called ultrafast diffusion exchange spectroscopy method shortens the experiment time by two to four orders of magnitude. Furthermore, because full 2D data are measured in a single scan (in a fraction of a second), the sensitivity of the experiment can be improved by several orders of magnitude using so-called nuclear spin hyperpolarization methods (in this case, dissolution dynamic nuclear polarization). As the first demonstration of the feasibility of the method in various applications, we show that the method enables quantification of intra-and extracellular exchange of water in a yeast cell suspension.