The role of pH in regulating and mediating processes in biological systems is nearly ubiquitous. Within the cell the pH changes from one compartment to another, and many processes, for example most of those involving endocytosis, are controlled or mediated by these pH changes. Examples include the release of folic acid from folic acid receptor, the membrane fusion processes that accompany viral infectivity, the onset of pH stress mediated chaperone activity in enteric bacteria such as E. coli. In order to understand such processes it is essential to be able to model protein folding and binding processes, as well as pH dependency of these phenomena. In this talk I will describe our development of approaches to treat the complex, pH-mediated process of the transformation between chaperone-inactive and chaperone active states of the small protein HdeA, which provides pH-stress to periplasmic proteins in enteric E. coli as these organisms transit through the human stomach. These methods integrate all atom constant pH approaches with coarse-grained folding/binding simulations to provide a detailed picture of the complex pH-dependent equilibrium that controls the chaperone activity of HdeA.<br/>

Multi-resolution modeling of protein folding and function of a pH-dependent chaperone

251st National Meeting (2016)

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