Related Experiment Video
Updated: Feb 12, 2026

Methods for the Self-integration of Megamolecular Biopolymers on the Drying Air-LC Interface
Published on: April 7, 2017
Adsorption of Denaturated Lysozyme at the Air-Water Interface: Structure and Morphology
Richard A Campbell1, Andrea Tummino1,2, Imre Varga2,3
1Institut Laue-Langevin , 71 avenue des Martyrs, CS 20156 , 38042 Grenoble Cedex 9, France.
Abstract:
The application of protein deuteration and high flux neutron reflectometry has allowed a comparison of the adsorption properties of lysozyme at the air-water interface from dilute solutions in the absence and presence of high concentrations of two strong denaturants: urea and guanidine hydrochloride (GuHCl). The surface excess and adsorption layer thickness were resolved and complemented by images of the mesoscopic lateral morphology from Brewster angle microscopy. It was revealed that the thickness of the adsorption layer in the absence of added denaturants is less than the short axial length of the lysozyme molecule, which indicates deformation of the globules at the interface. Two-dimensional elongated aggregates in the surface layer merge over time to form an extensive network at the approach to steady state. Addition of denaturants in the bulk results in an acceleration of adsorption and an increase of the adsorption layer thickness. These results are attributed to incomplete collapse of the globules in the bulk from the effects of the denaturants as a result of interactions between remote amino acid residues. Both effects may be connected to an increase of the effective total volume of macromolecules due to the changes of their tertiary structure, that is, the formation of molten globules under the influence of urea and the partial unfolding of globules under the influence of GuHCl. In the former case, the increase of globule hydrophobicity leads to cooperative aggregation in the surface layer during adsorption. Unlike in the case of solutions without denaturants, the surface aggregates are short and wormlike, their size does not change with time, and they do not merge to form an extensive network at the approach to steady state. To the best of our knowledge, these are the first observations of cooperative aggregation in lysozyme adsorption layers.
Related Concept Videos
Protein Denaturation
Protein-protein Interfaces
Protein-Protein Interfaces
Analyte Adsorption and Distribution
States of Water
Water freezes when the intermolecular forces are greater than the kinetic energy. Unlike most other substances, water is less dense in its solid state than in its liquid state. This is because each water molecule can form...
Water and Mineral Acquisition

