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In order to identify the indicators having world-wide standards for the assessment of scientific performances at the level of both individual and institutions normalized for disciplines, we have carried out a comparative analysis of the relative scientific and technological level of individual scientists and individual scientific institutions competing internationally for given fields, using alternative indicators all based on the number of publications and on their impact factors in international SCI journals properly ranked properly weighted for their position, number of coauthors and discipline using deciles. This study, contrary to some gloomy opinions, suggests that interesting conclusions can be drawn from the above indicators. The utilization of the chosen indicators, tested world-wide in real situations, appears capable to effectively and objectively assess institutions and individual university professors and researchers proving to be quite significant and should be used to provide computer-assisted evaluation criteria for either maintaining or upgrading the given position, maintaining or closing public Institutions, and filtering grant applications.

Ovotransferrin and lactoferrin are iron-binding proteins with antiviral and antibacterial activities related to natural immunity, showing marked sequence and structural homologies. The antiviral activity of two hen ovotransferrin fragments DQKDEYELL (hOtrf219–227) and KDLLFK (hOtrf269–301 and hOtrf633–638) towards Marek’s disease virus infection of chicken embryo fibroblasts is reported here. These fragments have sequence homology with two bovine lactoferrin fragments with antiviral activity towards herpes simplex virus, suggesting that these fragments could have a role for the exploitation of the antiviral activity of the intact proteins towards herpes viruses. NMR analysis showed that these peptides, chemically synthetized, did not possess any favourite conformation in solution, indicating that both the aminoacid sequence and the conformation they display in the intact protein are essential for the antiviral activity.

Three different approaches (propensity curve shifting, hydropathy index evaluation, and iterative attribution/ cancellation of secondary structure) to the use of secondary structure percentages derived from circular dichroism measurements to improve the success rate of a protein secondary structure prediction method, without using decision constants, are described and compared. Propensity-curve shifting appears to be the best-performing approach, bearing an increase of 5.3% in the success rate of single-residue structural prediction when exact information on the secondary structure, obtained by X-ray crystallography, is employed; with information of an accuracy comparable to that obtainable by circular dichroism, the improvement stays between 3.5 and 4.9%, for a three-state prediction. Although developed with circular dichroism in mind, the method can use percentages of secondary structure obtained by any other experimental methodology from which they can be inferred, for instance Raman spectroscopy and infrared spectroscopy.