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Effect of the Air-Water Interface on the Structure of Lysozyme in the Presence of Guanidinum Chloride

Perriman, Adam; Henderson, Mark; Evenhuis, Christian; McGillivray, Duncan; White, John

Description

We report observations of the changes in the surface structure of lysozyme adsorbed at the air-water interface produced by the chemical denaturant guanidinium chloride. A primary result is the durability of the adsorbed surface layer to denaturation, as compared to the molecule in the bulk solution. Data on the surface film were obtained from X-ray and neutron reflectivity measurements and modeled simultaneously. The behavior of lysozyme in G.HC1 solutions was determined by small-angle X-ray...[Show more]

dc.contributor.authorPerriman, Adam
dc.contributor.authorHenderson, Mark
dc.contributor.authorEvenhuis, Christian
dc.contributor.authorMcGillivray, Duncan
dc.contributor.authorWhite, John
dc.date.accessioned2015-12-10T22:25:44Z
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/1885/53612
dc.description.abstractWe report observations of the changes in the surface structure of lysozyme adsorbed at the air-water interface produced by the chemical denaturant guanidinium chloride. A primary result is the durability of the adsorbed surface layer to denaturation, as compared to the molecule in the bulk solution. Data on the surface film were obtained from X-ray and neutron reflectivity measurements and modeled simultaneously. The behavior of lysozyme in G.HC1 solutions was determined by small-angle X-ray scattering. For the air-water interface, determination of the adsorbed protein layer dimensions shows that at low to moderate denaturant concentrations (up to 2 mol L-1). there is no significant distortion of the protein's tertiary structure at the interface, as changes in the orientation of the protein are sufficient to model data. At higher denaturant concentrations, time-dependent multilayer formation occurred, indicating molecular aggregation at the surface. Methodologies to predict the protein orientation at the interface, based on amino acid residues' surface affinities and charge, were critiqued and validated against our experimental data.
dc.publisherAmerican Chemical Society
dc.sourceJournal of Physical Chemistry B
dc.subjectKeywords: Air; Enzymes; Solutions; Surface structure; X ray scattering; Air-water interface; Bulk solutions; Chemical-; Guanidinium chlorides; Small-angle x-ray scattering; Surface films; Surface layering; X-Ray and neutron reflectivity; Phase interfaces; guanidine
dc.titleEffect of the Air-Water Interface on the Structure of Lysozyme in the Presence of Guanidinum Chloride
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume112
dc.date.issued2008
local.identifier.absfor030403 - Characterisation of Biological Macromolecules
local.identifier.ariespublicationu4217927xPUB278
local.type.statusPublished Version
local.contributor.affiliationPerriman, Adam, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationHenderson, Mark, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationEvenhuis, Christian, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationMcGillivray, Duncan, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationWhite, John, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue31
local.bibliographicCitation.startpage9532
local.bibliographicCitation.lastpage9539
local.identifier.doi10.1021/jp800354r
dc.date.updated2015-12-09T09:27:06Z
local.identifier.scopusID2-s2.0-49649099750
local.identifier.thomsonID000258097700035
CollectionsANU Research Publications

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