OSA's Digital Library

Optics InfoBase > Conference Papers > FiO > 2004 > FTuE > Page FTuE2 © 2004 OSA

Conference Paper
Frontiers in Optics
Rochester, New York United States
October 12, 2004
ISBN: 1-55752-779-2
Current Trends in Biomedical Spectroscopy and Imaging I (FTuE)

Protein sensing with SERS: Insulin variants and phosphorylation detection

Eldar N. Khaliullin, Vladimir Drachev, Mark Thoreson, V. Jo Davisson, Meena Narsimhan, Dor Ben-Amotz, and Vladimir M. Shalaev

http://dx.doi.org/10.1364/FIO.2004.FTuE2


View Full Text Article

Acrobat PDF (100 KB) Note that full-text PDFs from conferences typically contain 1-3 pages of content, some or all of which might be an abstract, summary, or miscellaneous items.





Browse Journals / Lookup Meetings

Browse by Journal and Year


   


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

Share
Citations
  • Export Citation/Save Click for help

Abstract

Spectral differences of surface enhanced Raman scattering (SERS) were observed for human insulin versus analog and for phosphorylated protein versus unphosphorylated. Adaptive silver films enable soft protein deposition and improved SERS enhancement. This allows to detect small structural differences of proteins at sub-monolayer density.

© 2004 Optical Society of America

OCIS Codes
(170.6510) Medical optics and biotechnology : Spectroscopy, tissue diagnostics
(300.6330) Spectroscopy : Spectroscopy, inelastic scattering including Raman
(300.6450) Spectroscopy : Spectroscopy, Raman

Citation
E. N. Khaliullin, V. Drachev, M. Thoreson, V. Jo Davisson, M. Narsimhan, D. Ben-Amotz, and V. M. Shalaev, "Protein sensing with SERS: Insulin variants and phosphorylation detection," in Frontiers in Optics 2004/Laser Science XXII/Diffractive Optics and Micro-Optics/Optical Fabrication and Testing, OSA Technical Digest Series (Optical Society of America, 2004), paper FTuE2.
http://www.opticsinfobase.org/abstract.cfm?URI=FiO-2004-FTuE2


Sort:  Journal  |  Reset

References

References are not available for this paper.

OSA is a member of CrossRef.

CrossCheck Deposited