The analysis of the structural characteristics and dynamic properties of proteins is being done using a technology called hydrogen/deuterium exchange mass spectrometry, or HDX-MS. It might stand alone or work in conjunction with structural biology techniques such as cryo-electron microscopy (EM). Both small protein complexes and big protein aggregates may be studied using HDX-MS. Due to recent methodological developments and expanding equipment availability, HDX-MS is increasingly being used on a regular basis for various applications. Conformation and ligand interaction analyses by HDX-MS are already practically standard procedures when working with samples of low to medium complexity and sizes of less than 150 kDa. The quick development of the computational (software) backdrop, which makes it easier to analyse the data from the experiments, is another strong argument in favour of this. Analytes that are challenging to analyse with any other method can occasionally be handled using HDX-MS. This approach can also be used to analyse large complexes like viral capsids and disordered proteins. Given that it can now also analyse membrane proteins and post-translational changes, HDXMS has lately established itself as a reliable tool in the drug discovery and biopharmaceutical development processes (Hjortland et al., 1976).
Static high resolution structures have contributed significantly to our understanding of protein structure and mechanistic function. As structural biology progressed, it became clear that highresolution structures alone could not fully capture the mechanistic basis for protein structure and function in solution. Hydrogen/Deuteriumexchange Mass Spectrometry (HDXMS) has recently emerged as a powerful and versatile tool for structural biologists, providing novel insights into protein structure and function. HDXMS allows for direct monitoring of a protein's structural fluctuations and conformational changes in solution while it is performing its functions. Static highresolution structures have played a significant role in the development of our knowledge of protein structure and molecular function. High-resolution structures by themselves are unable to adequately reflect the molecular underpinnings of protein structure and function in solution; it has become abundantly obvious as structural biology has progressed. For structural biologists, Hydrogen/Deuterium-exchange Mass Spectrometry (HDX-MS) has recently grown into a potent and adaptable technology that offers fresh perspectives on the structure and function of proteins. When a protein is performing its functions in solution under native conditions, HDX-MS provides direct observation of structural fluctuations and conformational changes (Chaudhuri et al., 2015).
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