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Fast and accurate measurement of core body temperature is crucial for accidental hypothermia treatment. We have developed a novel light and small adapter to the headset jack of a mobile phone based on Android. It has been applied to measure temperature and set up automatic notifications (e.g. Global Positioning System coordinates to emergency services dispatcher, ECMO coordinator). Its validity was confirmed in comparison with Vital Signs Monitor Spacelabs Healthcare Elance 93300 as a reference method, in a series of 260 measurements in the temperature range of 10-42 °C. Measurement repeatability was verified in a battery of 600 measurements (i.e. 100 readings at three points of 10, 25, 42 °C for both esophageal and tympanic catheters). Inter-method difference of ≤0.5 °C was found for 98.5% for esophageal catheter and 100% for tympanic catheter measurements, with concordance correlation coefficient of 0.99 for both. The readings were almost completely repeatable with water bath measurements (difference of ≤0.5 °C in 10 °C: 100% for both catheters; in 25 °C: 99% for esophageal catheter and 100% tympanic catheter; in 42 °C: 100% for both catheters). This lightweight adapter attached to smartphone and standard disposable probes is a promising tool to be applied on-site for temperature measurement in patients at risk of hypothermia.

This paper presents a method for determining the structure of the early stage (ES) intermediate in the multistage protein folding process. ES structure is modeled on the basis of a limited conformational subspace of the Ramachandran plot. The model distinguishes seven structural motifs corresponding to seven local probability maxima within the limited conformational subspace. Three of these are assigned to well-defined secondary structures, while the remaining four are found to represent various types of random coils. The presented heuristic approach also provides insight into the reasons behind incorrect predictions occurring when the folding process depends on external factors (e.g., ligands, ions or other proteins) rather than on the characteristics of the backbone itself. The accuracy of the presented method is estimated at around 48 %.

The proteins composed of short polypeptides (about 70 amino acid residues) representing the following functional groups (according to PDB notation): growth hormones, serine protease inhibitors, antifreeze proteins, chaperones and proteins of unknown function, were selected for structural and functional analysis. Classification based on the distribution of hydrophobicity in terms of deficiency/excess as the measure of structural and functional specificity is presented. The experimentally observed distribution of hydrophobicity in the protein body is compared to the idealized one expressed by a three-dimensional Gauss function. The differences between these two distributions reveal the specificity of structural/functional characteristics of the protein. The residues of hydrophobicity deficiency versus the idealized distribution are assumed to indicate cavities with the potential to bind ligands, while the residues of hydrophobicity excess are interpreted as potentially participating in protein-protein complexation. The distribution of hydrophobicity irregularity seems to be specific for particular structures and functions of proteins. A comparative analysis of such profiles is carried out to identify the potential biological activity of proteins of unknown function.