Silks, like many other biomaterials, have a hierarchical structure. The primary structure is the amino acid sequence of its proteins (spidroin), mainly consisting of highly repetitive glycine and alanine blocks, which is why silks are often referred to as a block co-polymer. On a secondary structure level, the short side chained alanine is mainly found in the crystalline domains (beta sheets) of the nanofibril, glycine is mostly found in the so-called amorphous matrix consisting of helical and beta turn structures. It is the interplay between the hard crystalline segments, and the strained elastic semi-amorphous regions, that gives spider silk its extraordinary properties. Various compounds other than protein are used to enhance the fibre's properties. Pyrrolidine has hygroscopic properties which keeps the silk moist while also warding off ant invasion. It occurs in especially high concentration in glue threads. Potassium hydrogen phosphate releases hydrogen ions in aqueous solution, resulting in a pH of about 4, making the silk acidic and thus protecting it from fungi and bacteria that would otherwise digest the protein. Potassium nitrate is believed to prevent the protein from denaturing in the acidic milieu.