title: Membrane protein analysis using an improved peptic in-solution digestion protocol.
abstract: In the proteomic analysis of membrane proteins, less-specific proteases have become a promising tool to overcome fundamental limitations of trypsin with its unique specificity for basic residues. Pepsin is well-known to be utilized for specific applications that require acidic conditions, but in terms of membrane protein identification and characterization, it has been disregarded for the most part. This work presents an optimization of an existing peptic digest protocol for the analysis of membrane proteins using bacteriorhodopsin from purple membranes as reference.
authors.affiliation: Cluster of Excellence Macromolecular Complexes, Institute for Pharmaceutical Chemistry, Goethe-University, Frankfurt am Main, Germany.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Rietschel
authors.forename: Sandra
authors.initials: S
authors.lastname: Bornemann
authors.forename: Tabiwang N
authors.initials: TN
authors.lastname: Arrey
authors.forename: Dominic
authors.initials: D
authors.lastname: Baeumlisberger
authors.forename: Michael
authors.initials: M
authors.lastname: Karas
authors.forename: Bjoern
authors.initials: B
authors.lastname: Meyer
mesh_terms: D001436:Bacteriorhodopsins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D019617:Halobacterium salinarum / Q000737:chemistry*; D010434:Pepsin A / Q000378:metabolism; D018717:Purple Membrane / Q000737:chemistry*; D012997:Solvents; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D053719:Tandem Mass Spectrometry
chemical_list: D012997:Solvents; D001436:Bacteriorhodopsins; D010434:Pepsin A