This book discusses the European Union's approach to governance reform in its development assistance relationships with various groups of developing countries. A group of expert authors outline the general features of the position on governance taken by the EU, which is currently the major multilateral donor of development assistance, and discuss the implementation of EU policies in a set of cases: the group of African, Caribbean and Pacific (ACP) states, the New Partnership for Africa's Development (NEPAD), Southeastern Europe, Central Asia, the Euro-Mediterranean, Latin America and fragile states. The contributions to the book argue that the EU's position on governance reform, particularly since the adoption of the European Consensus on Development in 2005, has had distinctly neoliberal overtones. The EU's governance-related strategies have been instrumental to deepening market-based reform in aid-receiving countries. Policies on state-building adopted by the EU reflect mainly the interests of and ideas embraced by the EU and its member states. To an important extent, the rhetoric accompanying EU policies does not match with the political and social dynamics inherent in governance structures on the ground in many of its aid-recipient partner countries. This book was published as a special issue of Third World Quarterly.

Utilizing high speed computational methods to extrapolate to the rest of the protein universe, the knowledge accumulated on a subset of examples, protein bioinformatics seeks to accomplish what was impossible before its invention, namely the assignment of functions or functional hypotheses for all known proteins. The Ten Most Wanted Solutions in Protein Bioinformatics considers the ten most significant problems occupying those looking to identify the biological properties and functional roles of proteins. -Problem One considers the challenge involved with detecting the existence of an evolutionary relationship between proteins. -Two and Three studies the detection of local similarities between protein sequences and analysis in order to determine functional assignment. -Four, Five, and Six look at how the knowledge of the three-dimensional structures of proteins can be experimentally determined or inferred, and then exploited to understand the role of a protein. -Seven and Eight explore how proteins interact with each other and with ligands, both physically and logically. -Nine moves us out of the realm of observation to discuss the possibility of designing completely new proteins tailored to specific tasks. -And lastly, Problem Ten considers ways to modify the functional properties of proteins. After summarizing each problem, the author looks at and evaluates the current approaches being utilized, before going on to consider some potential approaches. introbul Features

Using a geometric perspective, Protein Geometry, Classification, Topology, and Symmetry reviews and analyzes the structural principals of proteins with the goal of revealing the underlying regularities in their construction. It also reviews computer methods for structure analysis and the automatic comparison and classification of these structures with an analysis of the statistical significance of comparing different shapes. Following an analysis of the current state of protein classification, the authors explore more abstract geometric and topological representations, including the occurrence of knotted topologies. The book concludes with a consideration of the origin of higher-level symmetries in protein structure. The authors focus on simple geometric methods that are deterministic rather than probabilistic and on the more abstract simplifications of protein structure that allow a better understanding of the overall fold of the structure. Most of the methods described in this book have corresponding computer programs. These can be found (as C source code) at the ftp site of the Division of Mathematical Biology at the National Institute for Medical Research. This collection of ideas contains pedagogical material that make it ideal for post-graduate courses as well as new ideas and results essential for researchers investigating protein structures.

Basics of proteins and proteomics techniques In-depth understanding of mass-spectrometry and quantitative proteomics An overview of interactomics and its application for translational research. Advancement in the field of proteomics and challenges in clinical applications.

Chemical and Functional Properties of Food Proteins presents the current state of knowledge on the content of proteins in food structures, the chemical, functional, and nutritive properties of food proteins, the chemical and biochemical modification of proteins in foods during storage and processing, and the mutagenicity and carcinogenicity of nitrogenous compounds. It emphasizes the structure-function relationship as well as the effects of practical conditions applied in food processing on the biochemical and chemical reactions in food proteins and food product quality.

The first ten chapters discuss structure-function relationships, methods of analysis of nitrogenous compounds, chemical and enzymatic modifications, nutritive roles, and mutagenicity and carcinogenicity of food proteins. The following six chapters describe the proteins of meat and fish, milk, eggs, cereals, legumes, oilseeds and single cell organisms, and present detailed information on the effects of conditions applied in storage and processing on the reactions in proteins and their impact on quality attributes of food products.

Intrinsically Disordered Proteins, Volume 611, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics of interest, including the Characterization of Structure-Function relationships in the intrinsically disordered protein complexin, Distances, distance distributions, and ensembles of IDPs from single-molecule FRET, Biophysical characterization of disordered protein liquid phases, The Use of Mass Spectrometry to Examine IDPs - Unique Insights and Caveats, Fluorescence Depolarization Kinetics to Study Conformational Preference, Structural Plasticity and Membrane Binding of Intrinsically Disordered Proteins, Characterizing the Function of Intrinsically Disordered Proteins in the Circadian Clock, and more.

Offers discussions on the chemical and physicochemical modification of proteins for the enhancement of surface activity and functional properties in a variety of systems. The volume provides examples of specific applications of modified proteins in gelation, emulsification, foaming, adsorption and surface tension reduction for use in the food, cosmetics, pharmaceutical, and surfactant manufacturing industries.

This book consists of a series of 82 precise, easy-to-read articles by internationally renowned scientists and emphasizes the practical approach to HPLC with minimal theory, although the underlying principles for peptide and protein separations are clearly expressed. All of the major modes of microbore, ultrafast and analytical HPLC are discussed, including size-exclusion, ion-exchange, reversed-phase, hydrophobic interaction, and affinity and immunoaffinity chromatography. A section on preparative HPLC, including displacement techniques, is also presented. Problem-solving approaches to the separation of various classes of biologically active peptides and proteins are thoroughly explored, while the importance of peptide standards for monitoring column performance and for optimizing separation conditions is emphasized. Several articles focus on the choice of the correct detection method (electrochemical, UV, fluorescence), as well as the need for a proper knowledge of approaches to column and instrument maintenance and trouble-shooting. A section on predictive approaches deals with both computer simulation of peptide separations and peptide structure. The book also includes complementary techniques to HPLC, as well as other useful applications of HPLC. It enables both novice and experienced chromatographers to realize the full potential of this extremely powerful technique, in the process making an important contribution to scientific literature.

This book explores the remarkable information correspondences and probability structures of proteins. Correspondences are pervasive in biochemistry and bioinformatics: proteins share homologies, folding patterns, and mechanisms. Probability structures are just as paramount: folded state graphics reflect Angstrom-scale maps of electron density. The author explores protein sequences (primary structures), both individually and in sets (systems) with the help of probability and information tools. This perspective will enhance the reader's knowledge of how an important class of molecules is designed and put to task in natural systems, and how we can approach class members in hands-on ways.

First published in 1991, Chemical Reagents for Protein Modification, 2nd Edition provides a unique combination of theoretical and practical considerations for the use of chemical reagents for site-specific modification of proteins. The book is divided into three sections, with the first section describing general techniques, including information on the organic chemistry of the various modification reactions; the separation and characterization of site-specific modified proteins, including applications to proteins separated by electrophoresis followed by blotting; the specific chemical cleavage of peptide bonds in proteins; the separation of peptides by high-performance liquid chromatography and electrophoresis; and the use of chemical reagents to assess conformational change in proteins. The second section provides an encyclopedic description of reagents and reactions for the site-specific modification of individual amino acid residues in proteins. The final section presents descriptions of the use of chemical reagents to label biologically significant sites in proteins, including enzyme active sites and the use of covalent cross-linking to measure protein-protein interactions. Particular emphasis is placed on the use of photoaffinity reagents. The book will be an extremely useful research tool for all investigators interested in the solution chemistry of proteins.

The use of the chemical modification of proteins has evolved over the past 80 years, benefiting from advances in analytical, physical, and organic chemistry. Over the past 30 years, the use of chemical reagents to modify proteins has been crucial in determining the function and structure of purified proteins. This groundbreaking work is part of the foundation of emerging disciplines of proteomics, chemical biology, structure biology, and chemical proteomics. Chemical Reagents for Protein Modification, Fourth Edition provides a comprehensive review of reagents used for the chemical modification of proteins, representing a major revision of the work presented in previous editions. The completely updated Fourth Edition is substantially larger and includes five new chapters: Alkylating Agents Acylating Agents Nitration and Nitrosylation Oxidation Modification of Proteins with Reducing Agents There is greatly increased coverage of the chemical modification of cysteine, which is critical for bioconjugate synthesis. The chapter on reduction also provides information necessary for bioconjugate synthesis as well as for the processing of inclusion bodies. The book places emphasis on conditions that affect the specificity of the chemical modification of proteins, such as solvent and temperature. The format has been markedly revised, presenting information based on the chemical nature of the modifying material and on the amino acid residue modified. This new version has increased significance to biopharmaceuticals. Much of the information is in tabular form, which enables the rapid location of cited material.

Basics of proteins and proteomics techniques In-depth understanding of mass-spectrometry and quantitative proteomics An overview of interactomics and its application for translational research. Advancement in the field of proteomics and challenges in clinical applications.

A Unified Microscopic Approach to Analyzing Complex Processes in Molecular Motors Motor Proteins and Molecular Motors explores the mechanisms of cellular functioning associated with several specific enzymatic molecules called motor proteins. Motor proteins, also known as molecular motors, play important roles in living systems by supporting cellular transport and force generation via the transformation of chemical energy into mechanical work. The book presents established results, theoretical methods, and experimental observations related to biological molecular motors. It uses fundamental physical-chemical concepts and methods to develop a systematic theoretical framework for understanding motor protein dynamics. The author introduces the main ideas using simple arguments that avoid heavy mathematical derivations in favor of more intuitive physical understanding. Although the book assumes some rudimentary knowledge of cell biology, calculus, and basic ideas from chemistry and physics, it gives explanations and derivations for most results. Accessible to students and researchers in a wide range of scientific fields, this book provides a unified molecular picture for analyzing motor proteins. It connects major experimental facts on molecular motors to principal theoretical concepts consistent with the fundamental laws of chemistry and physics.

Driven by the widespread growth of proteomic practices, protein separation techniques have been refined to minimize variability, optimize particular applications, and adapt to user preferences in the analysis of proteins. Separation Methods in Proteomics provides a comprehensive examination of all major separation techniques for proteomics research. Written as a compilation of hands-on methods exemplified by the work of several recognized leaders in the field, this book may serve as a guide for selection of the optimal separation strategies to solve particular biological problems. Recent progress in the development of robust analytical techniques and instrumentation has created the need for good quality biological samples that are subject to analysis. Emphasizing the importance of sample preparation, the book explains how proteomes can be divided into smaller, less complicated "subproteomes" for individual analysis. It also highlights several hybrid approaches that take into account protein interactions. Including applications of the separation methods currently employed in proteomic analyses for both clinical and basic research, Separation Methods in Proteomics contains practical information that can enhance the current and future endeavors of scientists in proteomics, genomics, transcriptomics, biomarker discovery, and drug discovery.

Although less common than -amino acids, non- -amino acids-where the amino group is not on the carbon immediately adjacent to the carboxyl group but is attached to another carbon in the chain (for example, the , , carbon)-are components of biologically important molecules, are significant in the pharmaceutical industry, and are useful starting materials for many areas of organic chemistry. Since the publication of the first edition of this book nearly 20 years ago, synthetic work devoted to the preparation of non- -amino acids has expanded greatly. Methods of Non- -Amino Acid Synthesis, Second Edition has been extensively rewritten and reorganized, providing an up-to-date review of strategies and methods for non- -amino acid synthesis, particularly those amino acids that are key synthetic intermediates or important compounds in their own right. It focuses on acyclic amino acids of C3-C10, but also aminoalkanoic carboxylic acids, aminoalkenoic acids, and aminoalkynoic acids. The new edition contains many updated references and has a greater emphasis on the biological importance of non- -amino acids. In addition to an array of synthetic methods, the book offers discussions on why non- -amino acids are important. The book covers synthetic methods that rely on substituent refunctionalization, the conversion of cyclic precursors to acyclic amino acids, conjugate addition reactions, and enolate anion reactions and condensation reactions that lead to non- -amino acids. It also examines reactions and strategies that lead to good diastereoselectivity and enantioselectivity during synthesis. A chapter devoted to biologically important amino acids includes separate sections on GABA, GABOB, carnitine, DAVA, statine, and other significant amino acids as well as a new section on peptides and proteins that contain non- -amino acids. The final chapter addresses aminocyclic and heterocyclic amino acids.

Using a geometric perspective, Protein Geometry, Classification, Topology, and Symmetry reviews and analyzes the structural principals of proteins with the goal of revealing the underlying regularities in their construction. It also reviews computer methods for structure analysis and the automatic comparison and classification of these structures with an analysis of the statistical significance of comparing different shapes. Following an analysis of the current state of protein classification, the authors explore more abstract geometric and topological representations, including the occurrence of knotted topologies. The book concludes with a consideration of the origin of higher-level symmetries in protein structure. The authors focus on simple geometric methods that are deterministic rather than probabilistic and on the more abstract simplifications of protein structure that allow a better understanding of the overall fold of the structure. Most of the methods described in this book have corresponding computer programs. These can be found (as C source code) at the ftp site of the Division of Mathematical Biology at the National Institute for Medical Research. This collection of ideas contains pedagogical material that make it ideal for post-graduate courses as well as new ideas and results essential for researchers investigating protein structures.

This book explores the remarkable information correspondences and probability structures of proteins. Correspondences are pervasive in biochemistry and bioinformatics: proteins share homologies, folding patterns, and mechanisms. Probability structures are just as paramount: folded state graphics reflect Angstrom-scale maps of electron density. The author explores protein sequences (primary structures), both individually and in sets (systems) with the help of probability and information tools. This perspective will enhance the reader's knowledge of how an important class of molecules is designed and put to task in natural systems, and how we can approach class members in hands-on ways.

This second edition of Protein Purification provides a guide to the major chromatographic techniques, including non-affinity absorption techniques, affinity procedures, non-absorption techniques and methods for monitoring protein purity. The new edition of the book has been organized to encourage incremental learning about the topic, starting with the properties of water, progressing through the characteristics of amino acids and proteins which relate to the purification process. There is an overview of protein strategy and equipment, followed by discussions and examples of each technique and their applications. The basic theory and simple explanations given in Protein Purification make it an ideal handbook for final year undergraduates, and postgraduates, who are conducting research projects. It will also be a useful guide to more experienced researchers who need a good overview of the techniques and products used in protein purification. Key Features * Guide to the major techniques used in protein purification * Includes flowcharts to help the reader slect the best purification strategy * Contains step-by-step protocols that guide the reader through each technique and its use * Includes exercises and solutions

The series Topics in Heterocyclic Chemistry presents critical reviews on present and future trends in the research of heterocyclic compounds. Overall the scope is to cover topics dealing with all areas within heterocyclic chemistry, both experimental and theoretical, of interest to the general heterocyclic chemistry community. The series consists of topic related volumes edited by renowned editors with contributions of experts in the field. All chapters from Topics in Heterocyclic Chemistry are published Online First with an individual DOI. In references, Topics in Heterocyclic Chemistry is abbreviated as Top Heterocycl Chem and cited as a journal.

Glutamine: Biochemistry, Physiology, and Clinical Applications describes the different functions of glutamine (Gln) in animals and humans. Gln is both a nutrient and a signaling molecule, and its functions go beyond those of a simple metabolic fuel or protein precursor. This book has gathered together, in an unbiased and critical manner, all the available evidence and research on Gln including pathology (neurological diseases, intestinal diseases, critical illness, and cancer), physiology (successful aging), catabolic states, immunity, and exercise. Special attention is given to the potential benefit of Gln in states of insulin resistance and the role of Gln as a "conditionally essential" amino acid. The contributors are either pioneers or experts in the area of Gln from all around the globe, including Australia, Brazil, Canada, Europe, China, and the United States. This book is a valuable source of information for nutrition scientists, medical doctors, sports scientists, food scientists, dietitians, and anyone interested in nutrition. It is also a valuable resource for students in these fields and will be an important addition to university libraries.

The activity of many biopharmaceutical polymers is dependent on conformation, and the next several years will see increased interest in the conformational analysis of these polymers resulting from the development of biosimilar or "follow-on" biological products. While a wide variety of approaches to analysis exists, finding the most viable ones would be much easier with a consolidated reference that details the benefits and cost of each approach, with an emphasis on real results and real products. Explores the Growing Role of Conformational Analysis in Comparing Generic Biopharmaceuticals Approaches to the Conformational Analysis of Biopharmaceuticals gathers the most useful techniques and methods into a single volume, putting the greatest emphasis on those approaches that have proven the most fruitful. Rather than cover specific uses of techniques in detail, this book provides commercial biotechnologists and researchers with the information and references they need to make good choices about the technology they choose to use. With a large number of references that direct readers to primary source material, it includes studies drawn from the gamut of current literature, covering physical methods, such as differential scanning calorimetry, light scanning, and analytical ultracentrifugation. It also addresses chemical methods, such as hydrogen-deuterium exchange and trace labeling, along with infrared, ultraviolet, and Raman spectroscopy. Written by Roger Lundblad, a true pioneer in protein science, this volume supplies the necessary information researchers need to access when deciding on the most cost-effective approach, including: Comparability of biopharmaceuticals Characterization of follow-on biologics Quality attributes of protein biopharmaceuticals Confrontational analysis of biopharmaceutical products With a clear focus on relevant commercial biotechnology, this book belongs on the shelves of those serious researchers who are paving the way for the next generation of biopharmaceutical polymers.

The Latest Developments on the Role of Dynamics in Protein Functions Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods presents modern biomolecular computational techniques that address protein flexibility/dynamics at all levels of theory. An international contingent of leading researchers in chemistry, physics, and biology show how these advanced methods provide insights into dynamic aspects of biochemical processes. A particular focus is on intrinsically disordered proteins (IDPs), which lack a well-defined three-dimensional structure and function as dynamic ensembles. The book covers a wide spectrum of dynamics, from electronic structure-based to coarse-grained techniques via multiscaling at different levels. After an introduction to dynamics and historical overview of basic methodologies, the book addresses the following issues: Is there a quantitative relationship between enzymatic catalysis and protein dynamics? Which are the functionally relevant motions of proteins? How can structural properties and partner recognition mechanisms of IDPs be simulated? How can we speed up molecular dynamics? How can we describe conformational ensembles by the synergistic effort of computations and experiments? While dynamics is now considered essential for interpreting protein action, it is not yet an integral component in establishing structure-function relationships of proteins. Helping to reshape this classical view in biochemistry, this groundbreaking book explores advances in computational methodology and contributes to the new, ensemble way of studying proteins.

This book is unique; the factual content and ideas it expounds are only just beginning to be touched upon in standard texts. Protein Electron Transfer is a major collaborative effort by leading experts and explores the molecular basis of the rapidly expan

Structural Glycobiology covers the experimental, theoretical, and alternative technologies used in the study of the structural basis for the diverse biological roles of carbohydrates. The book overviews the application of specialized technologies to the study of carbohydrates in biology, reviews relevant and current research in the field, and is illustrated throughout by specific examples of how research investigations have yielded key structural and associated biological data on carbohydrates and glycolipids. In particular, the book focuses on:

• X-ray crystallography and small-angle scattering, NMR, and cryo-electron microscopy techniques
• Theoretical (modeling-based) approaches, such as molecular mechanics, molecular dynamics, free energy calculations, and carbohydrate docking
• Alternative techniques for yielding structural information on carbohydrates from complex biological samples
• Carbohydrates in medicine, specifically in areas that have been directly impacted by our understanding of the structural role of carbohydrates in immune recognition: cancer, organ transplantation, and infection

The rapid advances in recombinant DNA technology and the increasing availability of peptides and proteins with therapeutic potential are a challenge for pharmaceutical scientists who have to formulate these compounds as drug products.

Pharmaceutical Formulation Development of Peptides and Proteins, Second Edition discusses the development of therapeutic peptides and proteins, from the production of active compounds via basic pre-formulation and formulation to the registration of the final product.

Providing integrated solutions, this book discusses:

• The synthesis of peptides and the biotechnological production of proteins through recombinant DNA technology
• The physicochemical characteristics and stability of peptides and proteins
• The formulation of proteins as suspensions, solutions, and (mostly freeze-dried) solids
• The opportunities and challenges of non-parenteral delivery of peptides and proteins
• Risk factors, specifically the development of an unwanted immune response
• A simulation approach to describe the fate of peptides and proteins upon administration to a biological system
• The documentation required to register a protein-based drug

Scientists in the pharmaceutical industry and academia as well as postgraduate students in pharmaceutical science will find this a valuable resource.