Methods in Protein Sequence Analysis

✍ Scribed by Brigitte Wittmann-Liebold, Lothar Matschull, Ulrike Pilling, Hans-Arthur Bradaczek (auth.), Dr. Hans Jörnvall, Dr. Jan-Olov Höög, Dr. Ann-Margreth Gustavsson (eds.)

• Publisher: Birkhäuser Basel
• Year: 1991
• Tongue: English
• Leaves: 396
• Series: Advances in Life Sciences
• Edition: 1
• Category: Library

✦ Synopsis

Methods in protein sequence analysis constitute important fields in rapid progress. We have experienced a continuous increase in analytical sensitivity coupled with decreases in time necessary for purification and analysis. Several generations of sequencers, liquid/solid/gas-phase, have passed by and returned in other shapes during just over two decades. Similarly, the introduction of HPLC permitted an enormous leap forward in this as in other fields of biochemistry, and we now start to see new major advances in purification/analysis through capillary electrophoresis. Furthermore, progress in the field of mass spectrometry has matched that in chemical analysis and we witness continuous development, now emphasizing ion spray and other mass spectrometric approaches. In short, protein analysis has progressed in line with other developments in modern science and constitutes an indispensable, integral part of present-day molecular biology. Even the available molecular tools, in the form of proteases with different specificities, have increased in number, although we still have far to go to reach an array of "restriction proteases" like the sets of nucleases available to the molecular geneticist. Of course, conferences have been devoted to protein sequence analysis, in particular the MPSA (Methods in Protein Sequence Analysis) series, of which the 8th conference took place in Kiruna, Sweden, July 1-6 1990. Again, we witnessed much progress, saw new instruments, and experienced further interpretational insights into protein mechanisms and functions.

✦ Table of Contents

Front Matter....Pages I-8
Modular Berlin Microsequencer for the Sequential Degradation of Proteins and Peptides from the Amino- and Carboxyl-Terminal End....Pages 9-21
C-Terminal Sequence Analysis....Pages 23-34
Chemical C-Terminal Sequencing....Pages 35-45
Extending the Performance of the Solid-Phase Protein Sequencer....Pages 47-54
Direct Microsequencing of Blotted and Covalently Attached Proteins in a Cross-Flow Reaction Chamber....Pages 55-66
Current Strategies for Microscale Purification of Protein and Peptides for Sequence Analysis....Pages 67-77
Capillary Electrophoresis: A New Dimension in the Separation Sciences....Pages 79-90
Structural Analysis of Membrane Proteins....Pages 91-101
Protein-Electroblotting and Microsequencing in Establishing Integrated Human Protein Databases....Pages 103-114
Comparison of the Blotting Efficiencies of Various PVDF Membranes....Pages 115-121
Sensitive Determination of Amino Acid Derivatives from N-Terminal Sequence Analysis....Pages 123-132
Amino Acid Analysis and Sequencing — What is State-of-the-Art?....Pages 133-141
Realistic Expectations for Amino Acid Analysis....Pages 143-150
A Protein Chemistry Approach to the Modelling of Integral Membrane Proteins....Pages 151-160
N-Terminal Acetylated Mitochondrial Aldehyde Dehydrogenase is Found in Fresh but not Frozen Liver Tissue....Pages 161-167
Elucidating Ligand Binding Sites in Polypeptides by Photoaffinity Labeling with Aryl Azides....Pages 169-176
Use of Thiopropyl-Sepharose 6B for Isolation and Structure-Functional Analysis of Thiol Proteins....Pages 177-185
Zinc Fingers Involved in MHC Class I Gene Regulation: Use of Synthetic Peptides for Structural Analysis....Pages 187-195
Hydrophobic Surfactant Proteins SP-B and SP-C: Special Analytical Problems....Pages 197-204
The Yeast Prohormone-Processing Kex2 Protease, an Enzyme with Specificity for Paired Basic Residues....Pages 205-214
Structures of Three Inhibitor Complexes of HIV-1 Protease....Pages 215-221
Protease Specificity and Protein Sequence Analysis....Pages 223-230
Cleavage-Sites in Protein Targeting Signals....Pages 231-238
Studies on a Dimeric Aspartic Protease from a Single Domain of Pepsin....Pages 239-248
LC/MS and LC/MS/MS Screening for the Sites of Post-Translational Modification in Proteins....Pages 249-256
Protein and Peptide Sequence Analysis by Tandem Mass Spectrometry in Combination with Either Capillary Electrophoresis or Micro-Capillary HPLC....Pages 257-266
Plasma Desorption Mass Spectrometry as a Tool for Characterization of Native and Modified Forms of Recombinant Polypeptides....Pages 267-274
Plasma Desorption Mass Spectrometry in Monitoring Peptide Synthesis and Phosphorylation Reactions....Pages 275-284
Repeating Domains in the Plasma Proteins Participating in Blood Coagulation and Fibrinolysis....Pages 285-292
Structural Analysis of the Glucocorticoid Receptor Protein....Pages 293-300
C1̄ Inhibitor: Structure, Genetic Variants and Serpin Homologies....Pages 301-311
Genetic Strategies for Protein Purification....Pages 313-320
The Prediction of the Secondary Structure of Proteins....Pages 321-332
A Computer Method of Finding Supersecondary Structures....Pages 333-342
Usefulness of the PIR Database for Protein Comparisons....Pages 343-352
The Structure and Post-Translational Modification of Lipoyl Domains in 2-Oxo Acid Dehydrogenase Multienzyme Complexes....Pages 353-362
Zinc Chemistry in Function and Structure of Zinc Proteins....Pages 363-372
Patterns of Sequence Variation in Families of Homologous Proteins....Pages 373-385
Protein Folding: Local Structures, Domains and Assemblies....Pages 387-396
Back Matter....Pages 397-398

✦ Subjects

Science, general