Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices.

ABSTRACT: Understanding the water sorption behavior of protein powders is important in applications such as the preservation of protein-based pharmaceuticals. Most globular proteins exhibit a characteristic sigmoidal water adsorption isotherm at ambient conditions. However, it is not well understood how water sorption behavior is influenced by intrinsic factors that are related to structural properties of proteins. We investigate computationally how structural constraints on proteins influence the water sorption isotherms of amorphous protein powders. Specifically, we study the effects of non-local disulfide linkages and backbone connectivity using pheromone ER-23 and lysozyme as model proteins. We find that non-local disulfide linkages can significantly restrict structural changes during hydration

SUBMITTER: Kim SB 

PROVIDER: S-EPMC5554179 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature