4 resultados para human activity recognition
em Cambridge University Engineering Department Publications Database
Resumo:
Temporal synchronization of multiple video recordings of the same dynamic event is a critical task in many computer vision applications e.g. novel view synthesis and 3D reconstruction. Typically this information is implied through the time-stamp information embedded in the video streams. User-generated videos shot using consumer grade equipment do not contain this information; hence, there is a need to temporally synchronize signals using the visual information itself. Previous work in this area has either assumed good quality data with relatively simple dynamic content or the availability of precise camera geometry. Our first contribution is a synchronization technique which tries to establish correspondence between feature trajectories across views in a novel way, and specifically targets the kind of complex content found in consumer generated sports recordings, without assuming precise knowledge of fundamental matrices or homographies. We evaluate performance using a number of real video recordings and show that our method is able to synchronize to within 1 sec, which is significantly better than previous approaches. Our second contribution is a robust and unsupervised view-invariant activity recognition descriptor that exploits recurrence plot theory on spatial tiles. The descriptor is individually shown to better characterize the activities from different views under occlusions than state-of-the-art approaches. We combine this descriptor with our proposed synchronization method and show that it can further refine the synchronization index. © 2013 ACM.
Resumo:
The specific recognition between monoclonal antibody (anti-human prostate-specific antigen, anti-hPSA) and its antigen (human prostate-specific antigen, hPSA) has promising applications in prostate cancer diagnostics and other biosensor applications. However, because of steric constraints associated with interfacial packing and molecular orientations, the binding efficiency is often very low. In this study, spectroscopic ellipsometry and neutron reflection have been used to investigate how solution pH, salt concentration and surface chemistry affect antibody adsorption and subsequent antigen binding. The adsorbed amount of antibody was found to vary with pH and the maximum adsorption occurred between pH 5 and 6, close to the isoelectric point of the antibody. By contrast, the highest antigen binding efficiency occurred close to the neutral pH. Increasing the ionic strength reduced antibody adsorbed amount at the silica-water interface but had little effect on antigen binding. Further studies of antibody adsorption on hydrophobic C8 (octyltrimethoxysilane) surface and chemical attachment of antibody on (3-mercaptopropyl)trimethoxysilane/4-maleimidobutyric acid N-hydroxysuccinimide ester-modified surface have also been undertaken. It was found that on all surfaces studied, the antibody predominantly adopted the 'flat on' orientation, and antigen-binding capabilities were comparable. The results indicate that antibody immobilization via appropriate physical adsorption can replace elaborate interfacial molecular engineering involving complex covalent attachments.