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Please use this identifier to cite or link to this item: http://arks.princeton.edu/ark:/88435/dsp01v979v553j
 Title: A Computational Investigation of the Origin of Hysteresis in Water Sorption Isotherms of Proteins Authors: Sparano, Evan Michael Advisors: Debenedetti, Pablo G. Department: Chemical and Biological Engineering Class Year: 2016 Abstract: Understanding the water sorption behavior of proteins is essential to many industrial applications such as the development of cosmetic products and the formulation of long-term preservation techniques of pharmaceutical proteins. Recent advances in computational simulation methods have allowed the systematic computation of water sorption isotherms of proteins. However, the underlying causes of the hysteresis between adsorption and desorption isotherms are not yet clearly understood. Using three model proteins (lysozyme, Trp-cage, and KAP8.1), I investigated the protein-water interactions at a microscopic scale, using metrics such as hydrogen bonding, radial distribution functions, and solvent-accessible surface area. Although these metrics do not explain the hysteresis when averaged over the entire protein surface, noticeable localized differences arise when these metrics are compared on a per-residue basis. These results suggest that hysteresis in water sorption isotherms is associated with local differences in hydration across the protein surfaces. Furthermore, the polar, especially charged, residues primarily contribute to the hysteresis, which are confirmed through mutation studies using Trp-cage. Extent: 42 pages URI: http://arks.princeton.edu/ark:/88435/dsp01v979v553j Type of Material: Princeton University Senior Theses Language: en_US Appears in Collections: Chemical and Biological Engineering, 1931-2016

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