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This volume presents detailed protocols for novel strategies and approaches to improve functional understanding of protein N- and C-terminal biology. Protein Terminal Profiling: Methods and Protocols addresses topics such as protease specificity profiling, N-terminal acetylation, assays to probe protease activity in cellular systems, protein N- and C-termini on a proteome-wide scale, and biochemical approaches to explain and examine extracellular protease activities. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. “br>Cutting-edge and thorough, Protein Terminal Profiling: Methods and Protocols is a valuable resource for researchers that focus on biochemistry and cell biology, and those who share a broad interest in protein functionality and protein modifications.
Modifications and Targeting of Protein Termini, Part B, Volume 686 in the Methods in Enzymology serial, highlights new advances in the field with this new volume presenting interesting chapters on a variety of timely topics, including In vitro production of N-degron fused proteins and its application, Identification of N-degrons and N-recognins using peptide pull-downs combined with quantitative mass spectrometry-based proteomics, Monitoring ADO-dependent proteolysis in cells using fluorescent reporter proteins, Monitoring the interactions between N-degrons and N-recognins of the Arg/N-degron pathway, Characterization and chemical modulation of p62/SQSTM1/Sequestosome-1 as an autophagic N-recognin of the Arg/N-degron pathway. Other chapters cover Analysis of higher plant N-degron pathway components and substrates via expression in S. cerevisiae, Building libraries to dissect terminal degrons with fluorescent timers, Affinity isolation and biochemical characterization of N-degron ligands using the N-recognin, ClpS, Probing the effects of N-terminal acetylation on a-synuclein structure, aggregation and toxicity, Increasing the coverage of the N-terminome with Lys-N Amino Terminal enrichment (LATE), and more. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in Methods in Enzymology serials - Updated release includes the latest information on Modifications and Targeting of Protein Termini
Hands-on researchers describe in step-by-step detail 73 proven laboratory methods and bioinformatics tools essential for analysis of the proteome. These cutting-edge techniques address such important tasks as sample preparation, 2D-PAGE, gel staining, mass spectrometry, and post-translational modification. There are also readily reproducible methods for protein expression profiling, identifying protein-protein interactions, and protein chip technology, as well as a range of newly developed methodologies for determining the structure and function of a protein. The bioinformatics tools include those for analyzing 2D-GEL patterns, protein modeling, and protein identification. All laboratory-based protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
The Ninth International Conference on Methods in Protein Sequence Analysis was held for the first time in Asia from September 20 to September 24, 1992 in Otsu (a city near Kyoto), Japan. Approximately 400 delegates attended the meeting. Forty papers were presented orally and 147 poster presentations were discussed. Academic sessions were held from early in the morning until late in the evening. We are confident that the Conference was successful in providing up-to-date information about methods in protein sequence analysis to all participants. Moreover, with the knowledge and understanding of the present standard of various methods of analysis that are being used and will be used, we were able to clarify areas that need to be evaluated, to be improved and be explored further. Major topics in the Conference mostly covered areas in the methodology of protein sequence analysis, such as: micropreparation and microsequencing of proteins, mass spectrometry, post-translational modification, prediction and database analysis, and analysis of protein structures of special interests. The evolution of genetic engineering in molecular biology has greatly accelerated the accumulation of knowledge on the amino acid sequence of novel proteins regardless of whether they are expressed or not expressed in living organisms. In the early stage of accumulation of structural information, the amino acid sequence itself is worthy of notice.
Proteolysis is an irreversible posttranslational modification affecting each and every protein from its biosynthesis to its degradation. Limited proteolysis regulates targeting and activity throughout the lifetime of proteins. Balancing proteolysis is therefore crucial for physiological homeostasis. Control mechanisms include proteolytic maturation of zymogens resulting in active proteases and the shut down of proteolysis by counteracting endogenous protease inhibitors. Beyond the protein level, proteolytic enzymes are involved in key decisions during development that determine life and death – from single cells to adult individuals. In particular, we are becoming aware of the subtle role that proteases play in signaling events within proteolysis networks, in which the enzymes act synergistically and form alliances in a web-like fashion. Proteases come in different flavors. At least five families of mechanistically distinct enzymes and even more inhibitor families are known to date, many family members are still to be studied in detail. We have learned a lot about the diversity of the about 600 proteases in the human genome and begin to understand their physiological roles in the degradome. However, there are still many open questions regarding their actions in pathophysiology. It is in this area where the development of small molecule inhibitors as therapeutic agents is extremely promising. Approaching proteolysis as the most important, irreversible post-translational protein modification essentially requires an integrated effort of complementary research disciplines. In fact, proteolytic enzymes seem as diverse as the scientists working with these intriguing proteins. This book reflects the efforts of many in this exciting field of research where team and network formations are essential to move ahead.
Furthering efforts to simulate the potency and specificity exhibited by peptides and proteins in healthy cells, this remarkable reference supplies pharmaceutical scientists with a wealth of techniques for tapping the enormous therapeutic potential of these molecules-providing a solid basis of knowledge for new drug design. Provides a broad, comprehensive overview of peptides and proteins as mediators of cell movement, proliferation, differentiation, and communication. Written by more than 50 leading international authorities, Peptides and Protein Drug Analysis discusses strategies for dealing with the complexity of peptides and proteins in conformational flexibility and amino acid sequence variability analyzes drug formulations facilitated by solid-phase peptide synthesis and recombinant DNA technology examines chemical purity analysis by high-pressure chromatographic, capillary electrophoretic, gel electrophoretic, and isoelectric focusing methods highlights drug design elements derived from protein folding, bioinformatics, and computational chemistry demonstrates uses of unnatural mutagenesis and combinatorial chemistry explores mass spectrometry, protein sequence, and carbohydrate analysis illustrates bioassays and other new functional analysis methods surveys spectroscopic techniques such as ultraviolet, fluorescence, Fourier transform infrared, and nuclear magnetic resonance (NMR) addresses ways of distinguishing between levels of therapeutic and endogenous agents in cells reviews structural analysis tools such as ultracentrifugation and light, X-ray, and neutron scattering and more! Featuring over 3400 bibliographic citations and more than 500 tables, equations, and illustrations, Peptide and Protein Drug Analysis is a must-read resource for pharmacists; pharmacologists; analytical, organic, and pharmaceutical chemists; cell and molecular biologists; biochemists; and upper-level undergraduate and graduate students in these disciplines.
Following the succesful publication of "Proteome and Protein Analysis" in 2000, which was based on a former MPSA (Methods in Protein Structure Analysis) conference, Methods in Proteome and Protein Analysis presents the most interesting papers from the 14th MPSA meeting. Major topics include: protein and peptide sample preparation and separation; new reagent for protein sequence analysis; mass spectrometry in protein research; analysis of posttranslational modification; protein-protein interaction using MALDI-MS; manipulation of genome or functional compositon trap; structure-function correlation study using optical biosensors of microcolorimetrical techniques; structural proteomics as NMR or fluorescence polarization study; the classification and prediction of structure or functional sites; in silico analysis of proteins and proteomes; increasing throughput and data quality for proteomics.
"Methods in Protein Sequence Analysis - 1988" - contains selected contributions on modern protein- analytical techniques as presented by speakers at the Seventh International Conference on "Methods in Protein Sequence Analysis", held from July 3rd to July 8th, 1988 in Berlin. The book contains information on new methodologies for sensitive amino acid analysis, N- and C-terminal sequence analysis, and protein and peptide purification. In addition recent mass spectrometric approaches are described, as an alter native technique to the common stepwise degradative sequence analysis of polypeptides by the Edman method. The book presents new possibilities in the design of sequencers and sophisticated equipment for the structural analysis of peptides and proteins. It describes practical approaches for the investigation of protein domains and protein complexes, and contains review chapters on the crystallization of cell organelles as well as on recent theoretical aspects of protein folding mechanisms. The nature of protein folding is not yet understood, but further advances in this area would greatly enhance our present knowledge of protein structure and function. Further, the book gives examples of the application of gene technology to protein characterization and to the design of new proteins. This enables new studies on the structure and function of proteins to be made, and opens up efficient approaches to the design of drugs.
A noncommercial protein sequencing instrument. Analysis of amino acid phenylthiohydantoins by gas chromatography. Advances in the gas chromatographic analysis of amino acid phenyl- and methyl-thiolhydantoins. Gas-liquid chromatography (GLC) of amino acid derivatives. Quantitative procedures for use with the Edman-Begg sequenator: partial sequences of two unusual immunoglobulin light chains, Rzf and Sac...