Calcium-ligand variants of the myocilin olfactomedin propeller selected from invertebrate phyla reveal cross-talk with N-terminal blade and surface helices.

Olfactomedins are a family of modular proteins found in multicellular organisms that all contain five-bladed β-propeller olfactomedin (OLF) domains. In support of differential functions for the OLF propeller, the available crystal structures reveal that only some OLF domains harbor an internal calcium-binding site with ligands derived from a triad of residues. For the myocilin OLF domain (myoc-OLF), ablation of the ion-binding site (triad Asp, Asn, Asp) by altering the coordinating residues affects the stability and overall structure, in one case leading to misfolding and glaucoma.

Optimal difference test sequence and power for discriminating soups of varying sodium content: DTFM version of dual-reference duo-trio with unspecified tetrad tests.

As sodium reduction has become very important in the food industry, various types of unspecified duo-trio tests have been studied to improve its efficiency for studying samples with high sodium content, and a constant-saltier-reference duo-trio test with dual reference, one reference in the first position and the second reference in the middle between the two test stimuli (DTFM), has been recommended. For the duo-trio test, a 'comparison of distance' (COD) strategy has been generally assumed. Yet, theoretically for DTFM, the 2-AFC reminder (2-AFCR) τ-strategy is also possible, which would make DTFM more efficient than the unspecified tetrad test.