β Scribed by Nielsen, Ida; Bentsen, Iben Bach; Lisby, Michael; Hansen, Sabine; Mundbjerg, Kamilla; Andersen, Anni H; Bjergbaek, Lotte
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Relatively conservative modifications of three proteins were carried out to alter their surface properties. The protein properties modified were hydrophobicity and charge. This was done by acylation of amino groups with anhydrides. For the hydrophobic modification experiments, two proteins (p-lactog
Two different series of hydrophobically modified proteins were partitioned in a number of aqueous two-phase systems (ATPS) to investigate the effect of hydrophobicity as a single property on partitioning. The modified proteins were derived from P-lactoglobulin and bovine serum albumin (BSA). Measure
A series of charge-modified thaumatins with different values of surface charge were partitioned in aqueous twophase systems (ATPS) to study the effect of surface charge as a single property on partitioning. Electrophoretic mobility of the proteins in titration curves was used as a measure of surface