The adsorbed conformation of globular proteins at the air/water interfaceLad, M.D., Birembaut, F., Matthew, J.M., Frazier, R. ORCID: https://orcid.org/0000-0003-4313-0019 and Green, R. J. (2006) The adsorbed conformation of globular proteins at the air/water interface. Physical Chemistry Chemical Physics, 8 (18). pp. 2179-2186. ISSN 1463-9076 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1039/b515934b Abstract/SummaryExternal reflection FTIR spectroscopy and surface pressure measurements were used to compare conformational changes in the adsorbed structures of three globular proteins at the air/water interface. Of the three proteins studied, lysozyme, bovine serum albumin and P-lactoglobulin, lysozyme was unique in its behaviour. Lysozyme adsorption was slow, taking approximately 2.5 h to reach a surface pressure plateau (from a 0.07 mM solution), and led to significant structural change. The FTIR spectra revealed that lysozyme formed a highly networked adsorbed layer of unfolded protein with high antiparallel beta-sheet content and that these changes occurred rapidly (within 10 min). This non-native secondary structure is analogous to that of a 3D heat-set protein gel, suggesting that the adsorbed protein formed a highly networked interfacial layer. Albumin and P-lactoglobulin adsorbed rapidly (reaching a plateau within 10 min) and with little chance to their native secondary structure.
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