Parametric surfaces are an essential modeling tool in computer aided design and movie production. Even though their use is well established in industry, generating ray-traced images adds significant cost in time and memory consumption. Ray tracing such surfaces is usually accomplished by subdividing the surfaces on the fly, or by conversion to a polygonal representation. However, on-the-fly subdivision is computationally very expensive, whereas polygonal meshes require large amounts of memory. This is a particular problem for parametric surfaces with displacement, where very fine tessellation is required to faithfully represent the shape. Hence, memory restrictions are the major challenge in production rendering. In this article, we present a novel solution to this problem. We propose a compression scheme for a priori Bounding Volume Hierarchies (BVHs) on parametric patches, that reduces the data required for the hierarchy by a factor of up to 48. We further propose an approximate evaluation method that does not require leaf geometry, yielding an overall reduction of memory consumption by a factor of 60 over regular BVHs on indexed face sets and by a factor of 16 over established state-of-the-art compression schemes. Alternatively, our compression can simply be applied to a standard BVH while keeping the leaf geometry, resulting in a compression rate of up to 2:1 over current methods. Although decompression generates additional costs during traversal, we can manage very complex scenes even on the memory restrictive GPU at competitive render times.

G protein coupled receptors (GPCRs) allow for the transmission of signals across biological membranes. For a number of GPCRs, this signaling was shown to be coupled to prior dimerization of the receptor. The chemokine receptor type 4 (CXCR4) was reported before to form dimers and their functionality was shown to depend on membrane cholesterol. Here, we address the dimerization pattern of CXCR4 in pure phospholipid bilayers and in cholesterol-rich membranes. Using ensembles of molecular dynamics simulations, we show that CXCR4 dimerizes promiscuously in phospholipid membranes. Addition of cholesterol dramatically affects the dimerization pattern: cholesterol binding largely abolishes the preferred dimer motif observed for pure phospholipid bilayers formed mainly by transmembrane helices 1 and 7 (TM1/TM5-7) at the dimer interface. In turn, the symmetric TM3,4/TM3,4 interface is enabled first by intercalating cholesterol molecules. These data provide a molecular basis for the modulation of GPCR activity by its lipid environment.