Motion parallax for 360° RGBD video

We present a method for adding parallax and real-time playback of 360° videos in Virtual Reality headsets. In current video players, the playback does not respond to translational head movement, which reduces the feeling of immersion, and causes motion sickness for some viewers. Given a 360° video and its corresponding depth (provided by current stereo 360° stitching algorithms), a naive image-based rendering approach would use the depth to generate a 3D mesh around the viewer, then translate it appropriately as the viewer moves their head. However, this approach breaks at depth discontinuities, showing visible distortions, whereas cutting the mesh at such discontinuities leads to ragged silhouettes and holes at disocclusions. We address these issues by improving the given initial depth map to yield cleaner, more natural silhouettes. We rely on a three-layer scene representation, made up of a foreground layer and two static background layers, to handle disocclusions by propagating information from multiple frames for the first background layer, and then inpainting for the second one. Our system works with input from many of today''s most popular 360° stereo capture devices (e.g., Yi Halo or GoPro Odyssey), and works well even if the original video does not provide depth information. Our user studies confirm that our method provides a more compelling viewing experience than without parallax, increasing immersion while reducing discomfort and nausea

Nuclear magnetic resonance of the filamentous bacteriophage fd.

The filamentous bacteriophage fd and its major coat protein are being studied by nuclear magnetic resonance (NMR) spectroscopy. 31P NMR shows that the chemical shielding tensor of the DNA phosphates of fd in solution is only slightly reduced in magnitude by motional averaging, indicating that DNA-protein interactions substantially immobilize the DNA packaged in the virus. There is no evidence of chemical interactions between the DNA backbone and the coat protein, since experiments on solid virus show the 31P resonances to have the same principle elements of its chemical shielding tensor as DNA. 1H and 13C NMR spectra of fd virus in solution indicate that the coat proteins are held rigidly in the structure except for some aliphatic side chains that undergo relatively rapid rotations. The presence of limited mobility in the viral coat proteins is substantiated by finding large quadrupole splittings in 2H NMR of deuterium labeled virions. The structure of the coat protein in a lipid environment differs significantly from that found for the assembled virus. Data from 1H and 13C NMR chemical shifts, amide proton exchange rates, and 13C relaxation measurements show that the coat protein in sodium dodecyl sulfate micelles has a native folded structure that varies from that of a typical globular protein or the coat protein in the virus by having a partially flexible backbone and some rapidly rotating aromatic rings