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    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. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.

    Citation

    Thirunavukkarasu Sivaraman. A Review on Computational Approaches for Analyzing Hydrogen- Deuterium (H/D) Exchange of Proteins. Protein and peptide letters. 2021;28(4):372-381

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    PMID: 33006533

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