Abstract
Neutron reflectivity profiles were obtained for spread layers of the protein bovine serum albumin (BSA) at the air/water interface at a surface pressure of 15 mN m −1. By the use of hydrogen—deuterium isotopic substitution in the subphase, and constrained model fitting, the distribution of protein at the interface has been determined. The simplest possible model consistent with the data is a two-layer model. The upper layer contains the major portion of the molecule which lies flat along the surface, consistent with the α-helix conformation, and the lower layer contains only 7% vol. of BSA and probably consists of a number of hydrophilic chains dangling down from the upper layer. The results also imply that some 30% wt. of the protein is lost to the subphase on initial spreading.
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