Scaled interfacial activity of proteins at the liquid-vapor interface

A. Krishnan, J. Sturgeon, Christopher Siedlecki, E. A. Vogler

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Interfacial activity of proteins at the liquid-vapor interfaces was investigated. Proteins appear more similar than dissimilar on a weight/volume basis whereas molarity scaling reveals a 'Traube-rule' ordering by molecular weight. The findings suggest that adsorption is substantially driven by solution concentration rather than diversity in protein amphilicity. Results show that concentration scaling substantially alters perception of protein interfacial activity.

Original languageEnglish (US)
Title of host publicationTransactions - 7th World Biomaterials Congress
Number of pages1
StatePublished - Dec 1 2004
EventTransactions - 7th World Biomaterials Congress - Sydney, Australia
Duration: May 17 2004May 21 2004

Publication series

NameTransactions - 7th World Biomaterials Congress

Other

OtherTransactions - 7th World Biomaterials Congress
CountryAustralia
CitySydney
Period5/17/045/21/04

All Science Journal Classification (ASJC) codes

  • Engineering(all)

Fingerprint Dive into the research topics of 'Scaled interfacial activity of proteins at the liquid-vapor interface'. Together they form a unique fingerprint.

  • Cite this

    Krishnan, A., Sturgeon, J., Siedlecki, C., & Vogler, E. A. (2004). Scaled interfacial activity of proteins at the liquid-vapor interface. In Transactions - 7th World Biomaterials Congress (Transactions - 7th World Biomaterials Congress).