Protein Deformation and Surfactancy at an Interface

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dc.contributor.authorHolt, Stephen
dc.contributor.authorMcGillivray, Duncan
dc.contributor.authorPoon, Simon
dc.contributor.authorWhite, John
dc.date.accessioned2015-12-13T23:15:30Z
dc.date.issued2000
dc.date.updated2015-12-12T08:43:50Z
dc.description.abstractThe deformation of a protein, myoglobin and two derivatives, apomyoglobin and peptide (1-55) has been studied at the air/water interface. The filled monolayer has been shown to have a thickness of ca. 16 Å for the three materials, despite the different t
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/1885/88916
dc.publisherAmerican Chemical Society
dc.sourceJournal of Physical Chemistry B
dc.subjectKeywords: Air; Deformation; Derivatives; Monolayers; Proteins; Surface active agents; Surface structure; Water; Apomyoglobin; Myoglobin; Peptide; Phase interfaces
dc.titleProtein Deformation and Surfactancy at an Interface
dc.typeJournal article
local.bibliographicCitation.lastpage7438
local.bibliographicCitation.startpage7431
local.contributor.affiliationHolt, Stephen, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationMcGillivray, Duncan, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationPoon, Simon, University of Melbourne
local.contributor.affiliationWhite, John, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidHolt, Stephen, u9708710
local.contributor.authoruidMcGillivray, Duncan, u3217395
local.contributor.authoruidWhite, John, u8506305
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030403 - Characterisation of Biological Macromolecules
local.identifier.ariespublicationMigratedxPub18781
local.identifier.citationvolume104
local.identifier.scopusID2-s2.0-0034247564
local.type.statusPublished Version

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