Characterizing The Effects Of Macromolecular Crowding On Protein Stability Dynamics And Function

The topics covered by this volume include: protein destabilization at low temperatures; engineering the stability and function of Gene V Protein; free energy balance in protein folding; modelling protein stability as a heteropolymer collapse; stability of alpha helices; protein stability with T4 Lysozyme.

Completely revised and expanded to reflect the latest advancements in the field, Polysaccharides: Structural Diversity and Functional Versatility, Second Edition outlines fundamental concepts in the structure, function, chemistry, and stability of polysaccharides and reveals new analytical techniques and applications currently impacting the cosmeti

Here, leading contributors from the forefront of this exciting technology present authoritative and timely reviews on the state of the art of biocatalysis. They cover the whole spectrum from the discovery of novel enzymes - by modern screening, evolutionary or immunological approaches - through immobilization techniques for technical processes, to their use in the asymmetric synthesis of important target compounds.

This book describes recent important advancements in protein folding dynamics and stability research, as well as explaining fundamentals and examining potential methodological approaches in protein science. In vitro, in silico, and in vivo method based research of how the stability and folding of proteins help regulate the cellular dynamics and impact cell function that are crucial in explaining various physiological and pathological processes. This book offers a comprehensive coverage on various techniques and related recent developments in the experimental and computational methods of protein folding, dynamics, and stability studies. The book is also structured in such a way as to summarize the latest developments in the fiddle and key concepts to ensure that readers can understand advanced concepts as well as the fundamental big picture. And most of all, fresh insights are provided into the convergence of protein science and technology. Protein Folding Dynamics and Stability is an ideal guide to the field that will be of value for all levels of researchers and advanced graduate students with training in biochemical laboratory research.

Proteins in living cells perform an enormous variety of processes, among these is protein self-assembly or aggregation. While many proteins self-assemble as part of healthy biological function, malfunctioning proteins which pathologically self-assemble have been linked to numerous neurodegenerative diseases like Huntington's, Parkinson's, and Alzheimer's. We investigate the role of macromolecular crowders and system volume in the process of protein self-assembly. We present three major studies in this thesis: two on the role of macromolecular crowders in the self-assembly of actin and amyloid proteins using differential rate equations, and one utilizing a stochastic approach to study the effects of system volume and particle number on protein aggregation, as well as how crowders can change the microscopic details of reaction dynamics. We develop a model for the inclusion of crowding effects in kinetic rate constants and show remarkable fits to existing data for actin and nine amyloid-forming proteins in the presence of macromolecular crowders. We also show how fluctuations and overall dynamics change with system size and in the presence of crowders, and develop a stochastic method for determining the prevalence of individual reaction mechanisms and how they evolve over time. This reaction frequency method provides unique insight into the dynamics of the system and can be used to explain why certain aggregating systems behave as they do, and why their behavior changes in various conditions. Stochastic approaches, such as Gillespie's algorithm, may be necessary for studying the behavior of proteins in cells, as volumes of micelles and cellular compartments can be as small as 1pL, thus fluctuations in particle number become relevant and continuous rate approaches become less accurate. We also present a tool for user-friendly simulation and visualization of stochastic models of protein aggregation.

Biophysical Characterization of Proteins in Developing Biopharmaceuticals, Second Edition, presents the latest on the analysis and characterization of the higher-order structure (HOS) or conformation of protein based drugs. Starting from the very basics of protein structure, this book explains the best way to achieve this goal using key methods commonly employed in the biopharmaceutical industry. This book will help today’s industrial scientists plan a career in this industry and successfully implement these biophysical methodologies. This updated edition has been fully revised, with new chapters focusing on the use of chromatography and electrophoresis and the biophysical characterization of very large biopharmaceuticals. In addition, best practices of applying statistical analysis to biophysical characterization data is included, along with practical issues associated with the concept of a biopharmaceutical’s developability and the technical decision-making process needed when dealing with biophysical characterization data. Presents basic protein characterization methods and tools applicable to (bio)pharmaceutical research and development Highlights the capabilities and limitations of each technique Discusses the underlining science of each tool Empowers industrial biophysical chemists by providing a roadmap for applying biophysical tools Outlines the needs for new characterization and analytical tools in the biopharmaceutical industry