Analysis of insoluble proteins. (April 2009)

• Record Type: Journal Article
• Authors: Trimpin, Sarah; Brizzard, Bill
• Is Part Of: Biotechniques. Volume 46:Number 5(2009)
• Page Start: 321
• Page End: 326
• Publication Date: 2009-04
• 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: 10.2144/000113135
• 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.