FAO/WHO GIFT (Global Individual Food consumption data Tool): a global repository for harmonised individual quantitative food consumption studies.

Knowing who eats what, understanding the various eating habits of different population groups, according to the geographical area, is critical to develop evidence-based policies for nutrition and food safety. The FAO/WHO Global Individual Food consumption data Tool (FAO/WHO GIFT) is a novel open-access online platform, hosted by FAO and supported by WHO, providing access to harmonised individual quantitative food consumption (IQFC) data, especially in low- and middle-income countries (LMIC). FAO/WHO GIFT is a growing repository, which will serve as the global FAO/WHO hub to disseminate IQFC microdata. Currently five datasets from LMIC are available for dissemination, and an additional fifty datasets will be made available by 2022. To facilitate the use of these data by policy makers, ready-to-use food-based indicators are provided for an overview of key data according to population segments and food groups. FAO/WHO GIFT also provides an inventory of existing IQFC data worldwide, which currently contains detailed information on 188 surveys conducted in seventy-two countries. In order for end-users to be able to aggregate the available data, all datasets are harmonised with the European Food Safety Authority's food classification and description system FoodEx2 (modified for global use). This harmonisation is aimed at enhancing the consistency and reliability of nutrient intake and dietary exposure assessments. FAO/WHO GIFT is developed in synergy with other global initiatives aimed at increasing the quality, availability and use of IQFC data in LMIC to enable evidence-based decision-making and policy development for better nutrition and food safety.

Organic molecular soft ferromagnetism in a fullerene c60.

The properties of an organic molecular ferromagnet [C(60)TDAE(0.86); TDAE is tetrakis(dimethylamino)ethylene] with a Curie temperature ;T(c) = 16.1 kelvin are described. The ferromagnetic state shows no remanence, and the temperature dependence of the magnetization below ;T(c) does not follow the behavior expected of a conventional ferromagnet. These results are interpreted as a reflection of a three-dimensional system leading to a soft ferromagnet.

The quaternary structure of chicken acetylcholinesterase and butyrylcholinesterase; effect of collagenase and trypsin.

Acetylcholinesterase (EC 3.1.1.7.; AChE) and butyrylcholinesterase (EC 3.1.1.8.; BuChE) from chicken muscle exist as sets of structurally homologous forms with very similar properties. The collagenase sensitivity and aggregation properties of the 'heavy' forms of both enzymes indicate that they possess a collagen-like tail, and their stepwise dissociation by trypsin confirms that they correspond to triple (A12) and double (A8) collagen-tailed tetramers. In addition to this dissociating effect, trypsin digests an important fraction of the catalytic units of AChE, in a progressive manner, removing as much as 30% of the enzyme's mass, without inactivation of the tetramers and of the tailed molecules. The trypsin-modified AChE forms closely resemble the corresponding mammalian AChE forms in their hydrodynamic properties. It is not known whether the trypsin-digestible peptides, which do not appear to be involved in the ionic or hydrophobic interactions of the enzymes, are a fragment of the catalytic subunit or whether they constitute distinct polypeptides.