Abstract
(Chemical Equation Presented) Delicate probing: When nanodisc assemblies are used to present membrane proteins on a biochip surface, interactions of these proteins can be studied by mass spectrometry. The method is illustrated with the protein rhodopsin, which is immobilized to a self-assembled monolayer by way of a his-tagged membrane scaffold protein. Upon activation of rhodopsin with light, the protein complex transducin binds and can be detected using SAMDI mass spectrometry.
Original language | English (US) |
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Pages (from-to) | 8796-8798 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 46 |
Issue number | 46 |
DOIs | |
State | Published - 2007 |
Funding
This work was supported by the National Heart, Lung, and Blood Institute (grants HL47887, HL47889, HL47890, HL47892, HL47902, HL55208, and R01 HL58329) and the General Clinic Research Centers Program (grants NCRR GCRC, M01 RR431, and M01 RR01346).
Keywords
- Biochips
- Mass spectrometry
- Monolayers
- Proteins
- Rhodopsin
ASJC Scopus subject areas
- Catalysis
- General Chemistry