Please use this identifier to cite or link to this item: https://doi.org/10.1063/1.1846153
DC FieldValue
dc.titleSelf-assembly of protein at aqueous solution surface in correlation to protein crystallization
dc.contributor.authorJia, Y.
dc.contributor.authorLiu, X.-Y.
dc.date.accessioned2014-10-16T09:40:30Z
dc.date.available2014-10-16T09:40:30Z
dc.date.issued2005-01-10
dc.identifier.citationJia, Y., Liu, X.-Y. (2005-01-10). Self-assembly of protein at aqueous solution surface in correlation to protein crystallization. Applied Physics Letters 86 (2) : 023903-1. ScholarBank@NUS Repository. https://doi.org/10.1063/1.1846153
dc.identifier.issn00036951
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/97886
dc.description.abstractThe assembly of lysozyme (hen egg white) at the surface of aqueous solution follows the same behaviors as amphiphilic molecules. The critical assembly concentration appearing in the protein solutions is found to coincide with the equilibrium concentration of protein crystals under given conditions. The crystallization of protein regarded as a typical case of protein self-assembly in three dimensions has been discussed. The result reveals also the correlation between protein crystallization and the two-dimensional self-assembly at the surface of substrates. It follows that the protein crystallization condition can be determined without protein crystals. © 2005 American Institute of Physics.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1063/1.1846153
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1063/1.1846153
dc.description.sourcetitleApplied Physics Letters
dc.description.volume86
dc.description.issue2
dc.description.page023903-1
dc.description.codenAPPLA
dc.identifier.isiut000226701500087
Appears in Collections:Staff Publications

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