Proteins interacting with diverse ligands - proteins, peptides or DNA - are the basic principles underlying many biological processes, such as antigen-antibody binding, signal transduction or receptor binding. The technique of oligopeptide synthesis on a cellulose membrane and the subsequent binding assays allow the investigation of protein interactions. A particular advantage of these peptide arrays (SPOT - technology) is the high number of oligopeptide probes that can be tested in parallel. Detailed protocols for peptide synthesis, and the analysis of protein-protein, protein-DNA interactions as well as epitope mapping are presented in this manual. It is ideally suited not only for basic research laboratories but also for diagnostic and therapeutic applications since many diseases are related to dysfunctions in protein recognition and binding.

Christopher Schirwitz's thesis focuses on improving the quality of in situ synthesized high-complexity peptide micro arrays. Micro arrays containing proteins or small protein fragments in the form of peptides have become of great interest in proteomic research. With the help of these microarrays a large number of potential target molecules can be screened for interaction with a probe in a short timeframe. However, protein and peptide micro arrays are still lagging behind oligonucleotide arrays in terms of density, quality and manufacturing costs. A new approach developed at the German Cancer Research Center (DKFZ) has improved the synthesis of high-density peptide arrays. The current technology is capable of producing arrays with up to 40,000 different peptides per square cm by means of micro particle-based solid phase peptide synthesis. However, in situ synthesis approaches bear a conceptual disadvantage: The quality of the peptides is dependent on the efficiency of the synthesis so that peptide fragments are present in the resulting array among the desired full-length peptides. In peptide-protein interaction studies such peptide fragments. The central achievement of this thesis is the development of a new method allowing for the fast one-step purification of entire arrays without loss of resolution or spatial information. Christopher Schirwitz's work has resulted in a number of publications in high ranking journals.

Since the publication of Atherton and Sheppard's volume, the technique of Fmoc solid-phase peptide synthesis has matured considerably and is now the standard approach for the routine production of peptides. The focus of this new volume is much broader, and covers the essential procedures.

During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed "inert. " This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu.

Edited by a leading authority in the field, the first book on this important and emerging topic provides an overview of the latest trends in sequence-controlled polymers. Following a brief introduction, the book goes on to discuss various synthetic approaches to sequence-controlled polymers, including template polymerization, genetic engineering and solid-phase chemistry. Moreover, monomer sequence regulation in classical polymerization techniques such as step-growth polymerization, living ionic polymerizations and controlled radical polymerizations are explained, before concluding with a look at the future for sequence-controlled polymers. With its unique coverage of this interdisciplinary field, the text will prove invaluable to polymer and environmental chemists, as well as biochemists and bioengineers.

Peptides play a decisive role in many physiological processes, whether as neurotransmitters, hormones or antibiotics. The rapid developments in peptide research over the past few decades make it almost impossible for newcomers to gain an overview. This means an easily comprehensible yet concise introduction is vital. This unique work covers all the important aspects of this wide-ranging field in one handy volume. On the basis of the fundamental chemical and structural properties of peptides, this reference runs the gamut from analysis, the occurrence and biological importance of peptides, via chemical, biochemical and genetic methods of peptide synthesis, right up to peptide libraries, peptide design and their role in drug research. Yet this book offers much more than a mere overview of the latest level of research. An encyclopedic appendix with valuable data on more than 500 biological relevant peptides and proteins, a comprehensive register and details of further literature references make this the ideal reference for all questions regarding peptide research. For newcomers and specialists alike. On the basis of the fundamental chemical and structural properties of peptides, this reference runs the gamut from analysis, the occurrence and biological importance of peptides.

Written by recognized experts in the study of proteins, Proteomics for Biological Discovery begins by discussing the emergence of proteomics from genome sequencing projects and a summary of potential answers to be gained from proteome-level research. The tools of proteomics, from conventional to novel techniques, are then dealt with in terms of underlying concepts, limitations and future directions. An invaluable source of information, this title also provides a thorough overview of the current developments in post-translational modification studies, structural proteomics, biochemical proteomics, microfabrication, applied proteomics, and bioinformatics relevant to proteomics. Presents a comprehensive and coherent review of the major issues faced in terms of technology development, bioinformatics, strategic approaches, and applications Chapters offer a rigorous overview with summary of limitations, emerging approaches, questions, and realistic future industry and basic science applications Discusses higher level integrative aspects, including technical challenges and applications for drug discovery Accessible to the novice while providing experienced investigators essential information Proteomics for Biological Discovery is an essential resource for students, postdoctoral fellows, and researchers across all fields of biomedical research, including biochemistry, protein chemistry, molecular genetics, cell/developmental biology, and bioinformatics.