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The spontaneous assembly of polypeptides through non-covalent interactions at physiological conditions is the main focus of the presented work and will be discussed from two different perspectives: (i) the interaction of peptide chains with themselves leading to formation of higher order structures (self-assembling peptides); (ii) the interaction of polypeptides with nano-sized surfaces (protein-nanoparticle interactions). Although self-assembling peptides are an important growing class of biomaterials, most of the works in this field have focused upon their various biomedical applications without highlighting the molecular mechanisms which result in their self-assembly into supra-molecular structures inside the body. Herein, through an in-depth thermodynamic analysis utilizing Isothermal Titration Calorimtry technique, the driving forces for self-assembly of ionic self-complementary peptide RADA4 and its variants were identified implying great contribution of molecular hydration and charge to the self-assembly process. Furthermore, the interfacial molecules involved in self-assembly of these molecules was experimentally quantified. It was found that appending five serine residues to C-terminus of RADA4 can overshadow the hydrophobic contribution of RADA segment leading to hydrogen bonding being the main driving force for self-assembly; while presence of 5 lysine residues inhibited RADA4 self-assembly. Secondly, the interaction of proteins with zwitterionic-modified nanoparticles (NPs) was investigated. Although widely studied, the underlying mechanism for the protein-repellent behavior of zwitterionic polymers is largely unknown. A set of thermodynamic investigations was performed to study the interaction of two model proteins (with distinctly different adsorption behaviour) with the surface of zwitterionic-modified silica nanoparticles. The nature of the interaction between proteins and polymer-modified nanoparticle was identified along with highlighting the main driving forces leading to their adsorption onto the nanoparticle's surface. Moreover, the impact of zwitterion's spacer length and end-group chemistry on thermodynamics of protein adsorption was analyzed. Overall, our results indicated that the main advantage of zwitterionic polymer modification of surfaces are: i) an increase in water molecules at the interface, ii) lack of counter-ion release from surfaces and iii) lower structural reorganization of the system upon protein-surface interaction. The findings presented in this work will fundamentally impact our understanding of nano-bio interfaces leading to development of more optimum nano-biomaterials in future.
This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.
Enrico Di Cera, a rising star in biophysics, has organized a superb group of authors to write substantial chapters covering the most exciting and central issues relating to the bioenergetic aspects of proteins, nucleic acids, and their interactions. Topics covered in this book are protein and nucleic acid folding and stability, enzyme-substrate interactions, prediction of the affinity of complexes, electrostatics, and non-equilibrium aspects of protein function. The breadth of the topics covered in this book illustrates the growing importance of thermodynamic approaches in the study of biological phenomena. The book should be of wide interest to biophysicists, biochemists, and structural biologists.
Volume 323 of Methods in Enzymology is dedicated to the energetics of biological macromolecules. Understanding the molecular mechanisms underlying a biological process requires detailed knowledge of the structural relationships within the system and an equally detailed understanding of the energetic driving forces that control the structural interactions. This volume presents modern thermodynamic techniques currently being utilized to study the energetic driving forces in biological systems. It will be a useful reference source and textbook for scientists and students whose goal is to understand the energetic relationships between macromoleculer structures and biological functions. This volume supplements Volumes 259 and Volume 295 of Methods in Enzymology. Key Features * Probing Stability of Helical Transmembrane Proteins * Energetics of Vinca Alkaloid Interactions with Tubulin * Deriving Complex Ligand Binding Formulas * Mathematical Modeling of Cooperative Interactions in Hemoglobin * Analysis of Interactions of Regulatory Protein TyrR with DNA * Parsing Free Energy of Drug-DNA Interactions * Use of Fluorescence as Thermodynamics Tool
The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. These methods look to answer: What are the sources of energy that drive the function? Which of the pathways are of biological significance? As the base of macromolecular structures continues to expand through powerful techniques of molecular biology, such as X-ray crystal data and spectroscopy methods, the importance of tested and reliable methods for answering these questions will continue to expand as well. This volume presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions. Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research Offers step-by-step lab instructions, including necessary equipment, from a global research community
"an impressive text that addresses a glaring gap in the teaching of physical chemistry, being specifically focused on biologically-relevant systems along with a practical focus.... the ample problems and tutorials throughout are much appreciated." –Tobin R. Sosnick, Professor and Chair of Biochemistry and Molecular Biology, University of Chicago "Presents both the concepts and equations associated with statistical thermodynamics in a unique way that is at visual, intuitive, and rigorous. This approach will greatly benefit students at all levels." –Vijay S. Pande, Henry Dreyfus Professor of Chemistry, Stanford University "a masterful tour de force.... Barrick's rigor and scholarship come through in every chapter." –Rohit V. Pappu, Edwin H. Murty Professor of Engineering, Washington University in St. Louis This book provides a comprehensive, contemporary introduction to developing a quantitative understanding of how biological macromolecules behave using classical and statistical thermodynamics. The author focuses on practical skills needed to apply the underlying equations in real life examples. The text develops mechanistic models, showing how they connect to thermodynamic observables, presenting simulations of thermodynamic behavior, and analyzing experimental data. The reader is presented with plenty of exercises and problems to facilitate hands-on learning through mathematical simulation. Douglas E. Barrick is a professor in the Department of Biophysics at Johns Hopkins University. He earned his Ph.D. in biochemistry from Stanford University, and a Ph.D. in biophysics and structural biology from the University of Oregon.
Progressively builds a deep understanding of macromolecular behavior Based on each of the authors' roughly forty years of biophysics research and teaching experience, this text instills readers with a deep understanding of the biophysics of macromolecules. It sets a solid foundation in the basics by beginning with core physical concepts such as thermodynamics, quantum chemical models, molecular structure and interactions, and water and the hydrophobic effect. Next, the book examines statistical mechanics, protein-ligand binding, and conformational stability. Finally, the authors address kinetics and equilibria, exploring underlying theory, protein folding, and stochastic models. With its strong emphasis on molecular interactions, Equilibria and Kinetics of Biological Macromolecules offers new insights and perspectives on proteins and other macromolecules. The text features coverage of: Basic theory, applications, and new research findings Related topics in thermodynamics, quantum mechanics, statistical mechanics, and molecular simulations Principles and applications of molecular simulations in a dedicated chapter and interspersed throughout the text Macromolecular binding equilibria from the perspective of statistical mechanics Stochastic processes related to macromolecules Suggested readings at the end of each chapter include original research papers, reviews and monographs, enabling readers to explore individual topics in greater depth. At the end of the text, ten appendices offer refreshers on mathematical treatments, including probability, computational methods, Poisson equations, and defining molecular boundaries. With its classroom-tested pedagogical approach, Equilibria and Kinetics of Biological Macromolecules is recommended as a graduate-level textbook for biophysics courses and as a reference for researchers who want to strengthen their understanding of macromolecular behavior.
Essential publication for researchers in all fields of life sciences. Key Features * Major topics covered include: * Deciphering rules of helix stability in peptides * Protein Folding in Membranes * Molecular Crowding * Study of the Bohr Effect in Hemoglobin Intermediates * Photoacoustic Calorimetry of Proteins * Theoretical Aspects of Isothermal Titration Calorimetry * Energetic Methods to Study Bifunctional Biotin Repressor.
In the past several years, there has been an explosion in the ability of biologists, molecular biologists and biochemists to collect vast amounts of data on their systems. Biothermodynamics, Part C presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions. The use of thermodynamics in biological research is used as an “energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. These methods look to answer: What are the sources of energy that drive the function? Which of the pathways are of biological significance? As the base of macromolecular structures continues to expand through powerful techniques of molecular biology, such as X-ray crystal data and spectroscopy methods, the importance of tested and reliable methods for answering these questions will continue to expand as well. Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research Offers step-by-step lab instructions, including necessary equipment, from a global research community
This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed. *Methods for Evaluating Cooperativity in a Dimeric Hemoglobin*Multiple-Binding of Ligands to a Linear Biopolymer*Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions*Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis