www.fsu.edu College of Medicine Home FSU COM Header
   www.FSU.edu  
 

 Biomedical Proteomics Laboratory »  Instrument resources | Instrument Reservations | Personnel | Core Labs

 


Biomedical Proteomics Laboratory
Surface Plasmon Resonance

Quick Links

College of Medicine Complex

 
Background and applications

Surface Plasmon ResonanceSurface plasmon resonance (SPR) is a chip-based technology for label-free studies of biomolecular interactions. Since SPR is based on measuring changes in refractive index resulting from macromolecular interactions at the gold interface of the chip, this method is amenable to colored, turbid or opaque samples.  Analyzed systems range from small molecules to proteins, nucleic acids, crude extracts, lipid vesicles, and whole cells. Detection is in real time.

Some of the applications include analysis of: 

  • kinetic rates of  reactions (rates of complex formation and dissociation)
  • affinity (the strength of binding)
  • concentration of purified protein, or protein in a complex mixture
  • binding partner identification ("ligand fishing")
  • biomolecular complex formation

Instrument specs

For technical information and specifications, see page 7 of the Biacore T-100 Product Information Sheet (2.0MB).

More information

See vendor's site: Biacore

Suggested Reading

  • Abdiche, Y. N., and Myszka, D. G. (2004) Probing the mechanism of drug/lipid membrane interactions using Biacore. Anal Biochem 328, 233-43.
  • Baird, C. L., Courtenay, E. S., and Myszka, D. G. (2002) Surface plasmon resonance characterization of drug/liposome interactions. Anal Biochem 310, 93-9.
  • Rich, R. L., Hoth, L. R., Geoghegan, K. F., Brown, T. A., LeMotte, P. K., Simons, S. P., Hensley, P., and Myszka, D. G. (2002) Kinetic analysis of estrogen receptor/ligand interactions. Proc Natl Acad Sci U S A 99, 8562-7.
  • Buijs, J., and Franklin, G. C. (2005) SPR-MS in functional proteomics. Brief Funct Genomic Proteomic 4, 39-47.
  • Cooper M.A.(2004) Advances in membrane receptor screening and analysis.  J Mol Recognit 17, 286-315.
  • Davis, T. M., and Wilson, W. D. (2001) Surface plasmon resonance biosensor analysis of RNA-small molecule interactions. Methods Enzymol 340, 22-51.
  • Karlsson, R. (2004) SPR for molecular interaction analysis: a review of emerging application areas. J Mol Recognit 17, 151-61.
  • Lee, H. J., Yan, Y., Marriott, G., and Corn, R. M. (2005) Quantitative functional analysis of protein complexes on surfaces. J Physiol 563, 61-71.
  • McDonnell, J. M. (2001) Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition. Curr Opin Chem Biol 5, 572-7.
  • Natsume, T., Nakayama, H., and Isobe, T. (2001) BIA-MS-MS: biomolecular interaction analysis for functional proteomics. Trends Biotechnol 19, S28-33.
  • Pattnaik, P. (2005) Surface plasmon resonance: applications in understanding receptor-ligand interaction. Appl Biochem Biotechnol 126, 79-92.
  • Piehler, J. (2005) New methodologies for measuring protein interactions in vivo and in vitro. Curr Opin Struct Biol 15, 4-14.

Protocols and proceduresSecure Site - Log in required

Any manuals posted here are EXCLUSIVELY for the use related to the instruments housed in the BPL. All copyrights apply.
 

 
Admissions | Directory | COM Intranet | Web Mail | Library | Employment | Contact Us | CDCS | Calendar | Copyright & Privacy