Analysis of insoluble proteins. (May 2009)

• Record Type: Journal Article
• Authors: Trimpin, Sarah; Brizzard, Bill
• Is Part Of: Biotechniques. Volume 46:Number 6(2009)
• Page Start: 409
• Page End: 419
• Publication Date: 2009-05
• Subjects: fusion tag -- recombinant protein -- solvent-free mass spectrometry -- MALDI -- IMS; Biology, Experimental -- Periodicals; Molecular biology -- Periodicals; Medical technology -- Periodicals; Biology, Experimental; Medical technology; Molecular biology; Clinical Laboratory Techniques -- Periodicals; Research -- Periodicals; Medical Laboratory Science -- Periodicals; Periodicals; Electronic journals; 570
• DOI: 10.2144/000113168
• Languages: English
• ISSNs: 0736-6205

Abstract

The analysis of insoluble proteins represents a major technical challenge for the field of proteomics. For example, membrane proteins are often insoluble in common solvents and represent 20–30% of the proteins encoded by the human genome. Chemical analysis on an individual basis is often required and is laborious and time-consuming. This review presents an overview of methods for purification of expressed proteins using fusion tags as well as methods for analysis of insoluble proteins by mass spectrometry with a goal of achieving high-throughput analysis.