Native state Hydrogen-Deuterium (H/D) exchange method has been used to study the
structures and the unfolding pathways for quite a number of proteins. The H/D exchange method is
generally monitored using nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry
(MS) techniques. NMR-assisted H/D exchange methods primarily monitor the residue level
fluctuation of proteins, whereas MS-assisted H/D exchange methods analyze multifold ensemble
conformations of proteins. In this connection, quite a large number of computational tools and algorithms
have been developed for processing and analyzing huge amount of the H/D exchange data
generated from these techniques. In this review, most of the freely available computational tools associated
with the H/D exchange of proteins have been comprehensively reviewed and scopes to improve/
develop novel computational approaches for analyzing the H/D exchange data of proteins
have also been brought into fore.
Keywords: Computational tools, free energy, H/D exchange, NMR, MS, protein stability and folding pathways.
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