The New Zealand Strong Motion Earthquake Recorder Network

The network of strong-motion earthquake recorders, maintained throughout New Zealand by the Engineering Seismology Section of the Department of Scientific and Industrial Research, is described. The instruments are either deployed as ground instruments to measure potential earthquake attack on structures, or in structures, e.g. buildings, dams and industrial installations, to record structural response. Details are given of installation of instruments , maintenance, laboratory work, record retrieval and digitisation, costs and staffing for the network. Future developments mooted include an improved digitising system, the introduction of an improved version of the existing mechanical-optical instrument in 1979, and, in the long term, the introduction of an entirely new digital recorder, having an electrical output from its accelerometers, which will make possible the transmission of data by telephone or radio link

Antibody light chain variable domains and their biophysically improved versions for human immunotherapy

We set out to gain deeper insight into the potential of antibody light chain variable domains (VLs) as immunotherapeutics. To this end, we generated a na\uefve human VL phage display library and, by using a method previously shown to select for non-aggregating antibody heavy chain variable domains (VHs), we isolated a diversity of VL domains by panning the library against B cell super-antigen protein L. Eight domains representing different germline origins were shown to be non-aggregating at concentrations as high as 450 \u3bcM, indicating VL repertoires are a rich source of nonaggregating domains. In addition, the VLs demonstrated high expression yields in E. coli, protein L binding and high reversibility of thermal unfolding. A side-by-side comparison with a set of non-aggregating human VHs revealed that the VLs had similar overall profiles with respect to melting temperature (Tm), reversibility of thermal unfolding and resistance to gastrointestinal proteases. Successful engineering of a non-canonical disulfide linkage in the core of VLs did not compromise the non-aggregation state or protein L binding properties. Furthermore, the introduced disulfide bond significantly increased their Tms, by 5.5-17.5 \ub0C, and pepsin resistance, although it somewhat reduced expression yields and subtly changed the structure of VLs. Human VLs and engineered versions may make suitable therapeutics due to their desirable biophysical features. The disulfide linkage-engineered VLs may be the preferred therapeutic format because of their higher stability, especially for oral therapy applications that necessitate high resistance to the stomach's acidic pH and pepsin. \ua9 2014 Landes Bioscience.Peer reviewed: YesNRC publication: Ye