Using Surface Plasmon Resonance to Study SH2 Domain-Peptide Interactions
- Author(s)
- Watson, GM; Gunzburg, MJ; Wilce, JA;
- Journal Title
- Methods in Molecular Biology
- Abstract
- Biosensor measurement using surface plasmon resonance enables precise evaluation of peptide-protein interactions. It is a sensitive technique that provides kinetic and affinity data with very little sample and without the need for analyte labels. Here, we describe its application for the analysis of peptide interactions with the Grb7-SH2 domain prepared with a GST-tag for tethering to the chip surface. This has been successfully and reliably used for direct comparison of a range of peptides under different solution conditions as well as direct comparison of peptides flowed over different related SH2 domains in real time. We have used the BIAcore system and describe both the methodology for data collection and analysis, with principles also applicable to other biosensor platforms.
- Publisher
- Springer Link
- Keywords
- *Surface Plasmon Resonance; *src Homology Domains; Data Collection; Kinetics; Peptides; GST fusion protein expression; Growth receptor-bound protein 7; Sensor chip preparation; Steady-state analysis; Surface plasmon resonance
- Research Division(s)
- Structural Biology
- PubMed ID
- 37668975
- Publisher's Version
- https://doi.org/10.1007/978-1-0716-3393-9_10
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2023-09-21 11:41:21
Last Modified: 2023-09-21 12:08:28