简介
Summary:
Publisher Summary 1
In 2002, Link (medicine, Vanderbilt U.) and LaBaer (medicine, Harvard U.), along with Philip Andrews (U. of Michigan) started the course to provide an intensive hands-on introduction to identifying, sequencing, and studying proteins. Each year, 16 students are selected to perform actual procedures and interpret the data. This laboratory manual contains step-by-step protocols for conducting most of the experiments they have taught over the first six years. Notes are included about techniques and specific product numbers to help students reproduce the experiments in their own laboratories. Annotation 漏2009 Book News, Inc., Portland, OR (booknews.com)
Publisher Summary 2
Based on a popular course at Cold Spring Harbor Laboratory, this new manual assembles cutting鈥揺dge protocols, helpful hints, and lecture notes to teach researchers from a variety of disciplines the essential methods of proteomics. It provides well鈥搃llustrated descriptions of experimental procedures, detailed protocols involving state鈥搊f鈥搕he鈥揳rt instrumentation, and lists of recommended Web sites and reading material. It can be used as the basis for a course or as a detailed bench manual, and is indispensable for those performing proteomic experiments.
目录
Table Of Contents:
Preface vii
Introduction 1(12)
EXPERIMENTS
Analysis of Whole-cell Lysates by Two-dimensional Gel Electrophoresis and MALDI Mass Spectrometry 13(24)
Purification of Protein Complexes for Mass Spectrometry Analysis 37(18)
Qualitative and Quantitative Measurement of Peptides with MALDI TOF/TOF Mass Spectrometry 55(14)
Analysis of Protein Complexes: High-sensitivity Liquid Chromatography Coupled with Tandem Mass Spectrometry 69(14)
Phosphopeptide Analysis Using IMAC and Mass Spectrometry 83(12)
Multidimensional Protein Identification Technology (MudPIT) Analysis of Whole-cell Lysates 95(8)
Quantitative Mass Spectrometry Analysis of Whole-cell Extracts (iTRAQ) 103(14)
Analysis and Validation of Tandem Mass Spectra 117(26)
High-throughput Cloning of ORFs: Assembling Large Sets of Expression Constructs 143(10)
Construction of Protein Microarrays: Nucleic Acid Programmable Protein Array (NAPPA) 153(22)
Using the Nucleic Acid Programmable Protein Array (NAPPA) for Identifying Protein-Protein Interactions 175(50)
APPENDICES
Setup and Demonstration of a Nanoelectrospray lonization (nanoESI) Source and Tandem Mass Spectrometry (MS/MS) 183(6)
Solution Protein Digest 189(4)
In-gel Trypsin Digest of Gel-fractionated Proteins 193(4)
Trichloroacetic Acid (TCA) Precipitation of Proteins 197(2)
Monoisotopic and Immonium Ion Masses of Amino Acids 199(2)
Dipeptide Masses of Amino Acids 201(2)
LTQ Instrument Methods 203(8)
Off-line Desalting of Peptide Mixtures 211(4)
Preparing Competent Cells 215(2)
DMA Quantification 217(2)
Cautions 219(6)
Index 225
Preface vii
Introduction 1(12)
EXPERIMENTS
Analysis of Whole-cell Lysates by Two-dimensional Gel Electrophoresis and MALDI Mass Spectrometry 13(24)
Purification of Protein Complexes for Mass Spectrometry Analysis 37(18)
Qualitative and Quantitative Measurement of Peptides with MALDI TOF/TOF Mass Spectrometry 55(14)
Analysis of Protein Complexes: High-sensitivity Liquid Chromatography Coupled with Tandem Mass Spectrometry 69(14)
Phosphopeptide Analysis Using IMAC and Mass Spectrometry 83(12)
Multidimensional Protein Identification Technology (MudPIT) Analysis of Whole-cell Lysates 95(8)
Quantitative Mass Spectrometry Analysis of Whole-cell Extracts (iTRAQ) 103(14)
Analysis and Validation of Tandem Mass Spectra 117(26)
High-throughput Cloning of ORFs: Assembling Large Sets of Expression Constructs 143(10)
Construction of Protein Microarrays: Nucleic Acid Programmable Protein Array (NAPPA) 153(22)
Using the Nucleic Acid Programmable Protein Array (NAPPA) for Identifying Protein-Protein Interactions 175(50)
APPENDICES
Setup and Demonstration of a Nanoelectrospray lonization (nanoESI) Source and Tandem Mass Spectrometry (MS/MS) 183(6)
Solution Protein Digest 189(4)
In-gel Trypsin Digest of Gel-fractionated Proteins 193(4)
Trichloroacetic Acid (TCA) Precipitation of Proteins 197(2)
Monoisotopic and Immonium Ion Masses of Amino Acids 199(2)
Dipeptide Masses of Amino Acids 201(2)
LTQ Instrument Methods 203(8)
Off-line Desalting of Peptide Mixtures 211(4)
Preparing Competent Cells 215(2)
DMA Quantification 217(2)
Cautions 219(6)
Index 225
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