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Activation of G-protein-coupled receptors (GPCRs) is mediated by molecular switches throughout the transmembrane region of the receptor. In this work, we continued along the path of a previous computational study wherein energy transport in the β2 Adrenergic Receptor (β2-AR) was examined and allosteric switches were identified in the molecular structure through the reorganization of energy transport networks during activation. In this work, we further investigated the allosteric properties of β2-AR, using Protein Contact Networks (PCNs). In this paper, we report an extensive statistical analysis of the topological and structural properties of β2-AR along its molecular dynamics trajectory to identify the activation pattern of this molecular system. The results show a distinct character to the activation that both helps to understand the allosteric switching previously identified and confirms the relevance of the network formalism to uncover relevant functional features of protein molecules. 

Abstract We consider a system of anisotropic plates in the three-dimensional continuum, interacting via purely hard core interactions. We assume that the particles have a finite number of allowed orientations. In a suitable range of densities, we prove the existence of a uni-axial nematic phase, characterized by long range orientational order (the minor axes are aligned parallel to each other, while the major axes are not) and no translational order. The proof is based on a coarse graining procedure, which allows us to map the plate model into a contour model, and in a rigorous control of the resulting contour theory, via Pirogov-Sinai methods.