Off-site ignition probability of flammable gases.

A key step in the assessment of risk for installations where flammable liquids or gases are stored is the estimation of ignition probability. A review of current modelling and data confirmed that ignition probability values used in risk analyses tend to be based on extrapolation of limited incident data or, in many cases, on the judgement of those conducting the safety assessment. Existing models tend to assume that ignition probability is a function of release rate (or flammable gas cloud size) alone and they do not consider location, density or type of ignition source. An alternative mathematical framework for calculating ignition probability is outlined in which the approach used is to model the distribution of likely ignition sources and to calculate ignition probability by considering whether the flammable gas cloud will reach these sources. Data are collated on the properties of ignition sources within three generic land-use types: industrial, urban and rural. These data are then incorporated into a working model for ignition probability in a form capable of being implemented within risk analysis models. The sensitivity of the model results to assumptions made in deriving the ignition source properties is discussed and the model is compared with other available ignition probability methods.

The fibrillar substructure of keratin filaments unraveled.

We show that intermediate-sized filaments reconstituted from human epidermal keratins appear unraveled in the presence of phosphate ions. In such unraveling filaments, up to four "4.5-nm protofibrils" can be distinguished, which are helically twisted around each other in a right-handed sense. Lowering the pH of phosphate-containing preparations causes the unraveling filaments to further dissociate into "2-nm protofilaments." In addition, we find that reconstitution of keratin extracts in the presence of small amounts of trypsin yields paracrystalline arrays of 4.5-nm protofibrils with a prominent 5.4-nm axial repeat. Limited proteolysis of intact filaments immobilized on an electron microscope grid also unveils the presence of 4.5-nm protofibrils within the filament with the same 5.4-nm axial repeat. These results, together with other published data, are consistent with a 10-nm filament model based on three distinct levels of helical organization: (a) the 2-nm protofilament, consisting of multi-chain extended alpha-helical segments coiled around each other; (b) the 4.5-nm protofibril, being a multi-stranded helix of protofilaments; and (c) the 10-nm filament, being a four-stranded helix of protofibrils.