The structure of insulin at the air/water interface: monomers or dimers?

The hydrophobic character of the air/water interface affects the oligomeric composition of insulin. By using interface-specific vibrational sum frequency spectroscopy and calculations of insulin monomer and dimer second-order nonlinear susceptibilities χ((2)), we show that insulin monomers segregate...

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Bibliographic Details
Published in:	Physical chemistry chemical physics : PCCP Vol. 16; no. 48; p. 26722
Main Authors:	Mauri, S, Weidner, T, Arnolds, H
Format:	Journal Article
Language:	English
Published:	England 01-01-2014
Subjects:	Air - analysis Humans Insulin - chemistry Models, Molecular Protein Conformation Protein Multimerization Surface Properties Water - chemistry
Online Access:	Get more information
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Summary:	The hydrophobic character of the air/water interface affects the oligomeric composition of insulin. By using interface-specific vibrational sum frequency spectroscopy and calculations of insulin monomer and dimer second-order nonlinear susceptibilities χ((2)), we show that insulin monomers segregate to the air/water interface.
ISSN:	1463-9084
DOI:	10.1039/c4cp04926h