By J. R. Chapman
John R. Chapman recreates the luck of his past acclaimed e-book (Protein and Peptide research via Mass Spectrometry, 1996) with a huge new selection of state-of-the-art equipment within the research of proteins and peptides. Contributed through well-established investigators, every one bankruptcy offers historical past info earlier than guiding the researcher step by step throughout the experimental technique, with specified directions to aid guarantee experimental luck. The purposes lined variety commonly and contain protein sequencing, higher-order constitution choice, epitope mapping, kinetics, quantitation, glycosylation research, and bacterial typing. Authoritative and eminently functional, Mass Spectrometry of Proteins and Peptides demonstrates the total scope of this flexible analytical procedure. All protein chemists and biochemists, in addition to bioanalytical scientists, who are looking to make the most those strong equipment of their paintings, will locate this ebook critical.
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Extra resources for Mass Spectrometry of Proteins and Peptides (Methods in Molecular Biology Vol 146)
Mass Spectrometry 1. Set the electrospray ionization source temperature to 50°C. Adjust the nebulizing nitrogen flow to ≈20 L/min and the drying gas flow to ≈150 L/min. Set the mass spectrometer to give a peak width at half-height of 1 mass unit. 32 Raftery Fig. 2. (A) C4 RP-HPLC chromatogram of thrombin cleavage products of GSTCP10 fusion protein. (B) SDS-PAGE analysis of isolated proteins. Lane 1, mol wt markers; lane 2, mutant rCP10; lane 3, rCP10; lane 4, CP10-homodimer; lane 5, GST (lanes 1–5 were silver stained); lane 6, mutant rCP10; lane 7, rCP10; lane 8, CP10homodimer; lane 9, fusion protein (lanes 6–9 were detected with an anti-CP10 antibody using enhanced chemiluminescence).
Et al. (1997) Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal. Chem. 69, 767–776. 13. Link, A. , J. R. (1997) A strategy for the identification of proteins localized to subcellular spaces: application to E. coli periplasmic proteins. Int. J. Mass Spectrom. Ion Proc. 160, 303–316. 14. Larmann, J. , Lemmo, A. , Moore, A. , and Jorgenson, J. W. (1993) Two-dimensional separations of peptides and proteins by comprehensive liquid chromatography-capillary electrophoresis.
HPLC Columns 1. 0 mm × 25 cm (Vydac, Hesperia, CA). 2. 0 mm × 25 cm (PolyLC, Columbia, MD). 8. Micro-HPLC Columns 1. 100-µm ID × 360-µm OD fused-silica capillary (J+W Scientific, Folsom, CA). 2. 50-µm ID × 360-µm OD fused-silica capillary, ≈30 cm length (J+W Scientific). 3. Reversed-phase packing material (POROS R2, Perseptive Biosystems). Other C18 materials are also suitable. 4. PEEK micro cross (Upchurch, Oak Harbor, WA). 5. 025-in. diameter gold wire (Scientific Instruments Service, Ringoe, NY).