Microarrays for Amino Acid Analysis and Protein Sequencing
Edward Shipwash
Abstract
A method is described where the aminoacyl-tRNA synthetase system is used to create very small devices for quantitative analysis of the amino acids that occur in proteins. The basis of the method is that each of the 20 synthetases and/or a tRNA specific for a different amino acid is separated spatially (e.g. in tiny chambers or on a surface). The reactions catalyzed by all 20 synthetases are monitored in a spatially resolved manner. Each separately positioned synthetase or tRNA will signal its cognate amino acid. The synthetase reactions can be monitored using continuous spectroscopic assays. Alternatively, since elongation factor Tu;GTP (EF-Tu;GTP) specifically binds all AA-tRNAs, the aminoacylation reactions catalyzed by the synthetases can be monitored using ligand assays. Microarrays for amino acid analysis are suggested. Additionally, it is possible that amino acid analysis arrays can be integrated with aminopeptidase or carboxypeptidase digestions to produce miniaturized enzymatic sequenators capable of generating either N- or C-terminal sequence data at femtomole-attomole levels. The possibility of parallel processing of many samples in an automated manner is discussed.
Create a lesson
Related papers
Sensing via whole-body interactions with complex terrains: physical insights from robotic models
Chen Li
Efficient Transport Networks through Edge Pruning by Relative Resistance
Mathieu Le Verge-Serandour, Viktor Vasilev, Lara Szeimies et al.
Boundary-contact repolarization provides a mechanism for directional guidance of neural crest cell collectives
Aditya Shankar Paspunurwar, Hector Gomez
Femtosecond Three-Dimensional Imaging of Single-Protein with Hard X-ray Laser
Paul Lourdu Xavier, Andrew J. Morgan, Johan Bielecki et al.
Three-dimensional imaging of isolated membrane-protein complexes in vacuo with an X-ray laser
Kartik Ayyer, Tej Varma Yenupuri, Johan Bielecki et al.
Polarization of the Drosophila oocyte by active cortical exchange
Mohammadhossein Firouznia, Wen Lu, Margot Lakonishok et al.