CD spectroscopy of proteins adsorbed at flat hydrophilic quartz and hydrophobic Teflon surfaces

Citation
Awp. Vermeer et W. Norde, CD spectroscopy of proteins adsorbed at flat hydrophilic quartz and hydrophobic Teflon surfaces, J COLL I SC, 225(2), 2000, pp. 394-397
Citations number
17
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF COLLOID AND INTERFACE SCIENCE
ISSN journal
00219797 → ACNP
Volume
225
Issue
2
Year of publication
2000
Pages
394 - 397
Database
ISI
SICI code
0021-9797(20000515)225:2<394:CSOPAA>2.0.ZU;2-U
Abstract
Spectroscopic methods provide a powerful tool for studying the properties o f proteins at interfaces. The protein accumulated in one adsorbed layer is frequently less than the minimum mass of protein required by a detection me thod. In such a case las is the case in circular dichroism spectroscopy) th e sorbent material is usually supplied as dispersion. However, light scatte ring by the dispersed particles often interferes with the measurement of th e circular dichroism of the protein. Therefore, there is a strong need for an experimental setup that enables these measurements to be made using flat surfaces. An example of such a setup is the multiplate quartz cell present ed here. The potential of this multiplate quartz cell is shown by some prel iminary circular dichroism measurements of IgG adsorbed on different types of surfaces. (C) 2000 Academic Press.