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Proteins perform various functions in living organisms. However, any mutation in the amino acid residues of a protein affects its structure and function. Some of these mutations may lead to diseases. These disease-causing mutations have an impact on protein structure, stability, and its binding affinity to complexes. Moreover, the study of amino acid mutation in proteins is important for developing therapeutic strategies. It is a pertinent and timely endeavor to provide comprehensive insights on the consequences of these mutations.The main highlights of this book are the effects of protein mutations on its various functions such as aggregation, folding, stability, binding affinity, and diseases, as well as a wide range of applications such as database development, computational algorithms, and drug design. It will be a platform to provide the up-to-date information and latest developments in the field and will serve as a single resource to get the information on comparative studies to delineate these mutational effects on protein folding, stability, and interactions, and for understanding the molecular basis of diseases.
Each cell depends on thousands of proteins to do their jobs in the right places at the right times, to function correctly Sometimes, gene mutations prevent one or more of these proteins from working properly. By changing a gene’s instructions for making a protein, a mutation can cause the protein to malfunction or to be missing entirely. When a mutation alters a protein that plays a critical role in the body, it can disrupt normal development or cause a medical condition. A condition caused by mutations in one or more genes is called a genetic disorder. In some cases, gene mutations are so severe that they prevent an embryo from surviving until birth. · These changes occur in genes that are essential for development, and often disrupt the development of an embryo in its earliest stages. · Because these mutations have very serious effects, they are incompatible with life. It is important to note that genes themselves do not cause disease—genetic disorders are caused by mutations that make a gene function improperly. · For example, when people say that someone has the “cystic fibrosis gene,” they are usually referring to a mutated version of the CFTR gene, which causes the disease. · All people, including those without cystic fibrosis, have a version of the CFTR gene An attempt has been made in this informative Booklet to summarize the fundamental topics related to genetic mutations and its impact on health and development along with several illustrations. …Dr. H. K. Saboowala. M.B.(Bom) .M.R.S.H.(London)
As the tools and techniques of structural biophysics assume greater roles in biological research and a range of application areas, learning how proteins behave becomes crucial to understanding their connection to the most basic and important aspects of life. With more than 350 color images throughout, Introduction to Proteins: Structure, Function, and Motion presents a unified, in-depth treatment of the relationship between the structure, dynamics, and function of proteins. Taking a structural–biophysical approach, the authors discuss the molecular interactions and thermodynamic changes that transpire in these highly complex molecules. The text incorporates various biochemical, physical, functional, and medical aspects. It covers different levels of protein structure, current methods for structure determination, energetics of protein structure, protein folding and folded state dynamics, and the functions of intrinsically unstructured proteins. The authors also clarify the structure–function relationship of proteins by presenting the principles of protein action in the form of guidelines. This comprehensive, color book uses numerous proteins as examples to illustrate the topics and principles and to show how proteins can be analyzed in multiple ways. It refers to many everyday applications of proteins and enzymes in medical disorders, drugs, toxins, chemical warfare, and animal behavior. Downloadable questions for each chapter are available at CRC Press Online.
Genetic variations may change the structure and function of individual proteins as well as affect their interactions with other proteins and thereby impact metabolic processes dependent on protein-protein interactions. For example, cytochrome P450 proteins, which metabolize a vast array of drugs, steroids and other xenobiotics, are dependent on interactions with redox and allosteric partner proteins for their localization, stability, (catalytic) function and metabolic diversity (reactions). Genetic variations may impact such interactions by changing the splicing and/or amino acid sequence which in turn may impact protein topology, localization, post translational modifications and three dimensional structure. More generally, research on single gene defects and their role in disease, as well as recent large scale sequencing studies suggest that a large number of genetic variations may contribute to disease not only by affecting gene function or expression but also by modulating complex protein interaction networks. The aim of this research topic is to bring together researchers working in the area of drug, steroid and xenobiotic metabolism who are studying protein-protein interactions, to describe their recent advances in the field. We are aiming for a comprehensive analysis of the subject from different approaches including genetics, proteomics, transcriptomics, structural biology, biochemistry and pharmacology. Of particular interest are papers dealing with translational research describing the role of novel genetic variations altering protein-protein interaction. Authors may submit original articles, reviews and opinion or hypothesis papers dealing with the role of protein-protein interactions in health and disease. Potential topics include, but are not limited to: • Role of protein-protein interactions in xenobiotic metabolism by cytochrome P450s and other drug metabolism enzymes. • Role of classical and novel interaction partners for cytochrome P450-dependent metabolism which may include interactions with redox partners, interactions with other P450 enzymes to form P450 dimers/multimers, P450-UGT interactions and proteins involved in posttranslational modification of P450s. • Effect of genetic variations (mutations and polymorphisms) on metabolism affected by protein-protein interactions. • Structural implications of mutations and polymorphisms on protein-protein interactions. • Functional characterization of protein-protein interactions. • Analysis of protein-protein interaction networks in health and disease. • Regulatory mechanisms governing metabolic processes based on protein-protein interactions. • Experimental approaches for identification of new protein-protein interactions including changes caused by mutations and polymorphisms.
This book is indexed in Chemical Abstracts ServiceThe interactions of proteins with other molecules are important in many cellular activities. Investigations have been carried out to understand the recognition mechanism, identify the binding sites, analyze the the binding affinity of complexes, and study the influence of mutations on diseases. Protein interactions are also crucial in structure-based drug design.This book covers computational analysis of protein-protein, protein-nucleic acid and protein-ligand interactions and their applications. It provides up-to-date information and the latest developments from experts in the field, using illustrations to explain the key concepts and applications. This volume can serve as a single source on comparative studies of proteins interacting with proteins/DNAs/RNAs/carbohydrates and small molecules.
The Protein Data Bank (PDB; http://wwpdb.org) was established in 1971 as the first open access digital data resource in biology with seven protein structures as its initial holdings. The global PDB archive now contains more than 124,000 experimentally determined atomic level 3D structures of biological macromolecules, all of which are freely accessible via the Internet. Knowledge of the 3D structure of a gene product is beneficial for understanding its function and its role in disease. The main theme of this thesis is to improve our knowledge of this relationship between genes and proteins. First, we manually review the existing knowledge of how changes in 3D protein structure are related to diseases. Second, we analyze novel datasets of genetic information and prioritize single nucleotide variation for further analysis, using protein level annotations. Of particular interest in the PDB archive are protein structures for which 3D structures of both wild type and genetic variants have been determined, thereby revealing atomic-level structural differences. In the first part of this thesis, we present a systematic review of these cases. We observe a wide range of possible structural and functional changes at the protein caused by single point mutations, including changes in enzyme activity, aggregation, structural stability, binding and dissociation, some in the context of large biological assemblies. An increasing number of software methods are available that attempt to predict the consequences of genetic variation data. Our results show that the range of possible consequences is much larger than is often assumed and also a comprehensive understanding of three-dimensional structure, dynamics, and biophysics will be required to develop better tools that can make accurate predictions about the consequences of genetic changes manifested at the atomic level in protein and RNA gene products. In the second part of this thesis, we are developing a bioinformatics pipeline by which we can achieve fast and accurate annotation for large variation databases using information derived from protein sequences and 3D structures.
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.
This book is the seventh in a series of titles from the National Research Council that addresses the effects of exposure to low dose LET (Linear Energy Transfer) ionizing radiation and human health. Updating information previously presented in the 1990 publication, Health Effects of Exposure to Low Levels of Ionizing Radiation: BEIR V, this book draws upon new data in both epidemiologic and experimental research. Ionizing radiation arises from both natural and man-made sources and at very high doses can produce damaging effects in human tissue that can be evident within days after exposure. However, it is the low-dose exposures that are the focus of this book. So-called “late” effects, such as cancer, are produced many years after the initial exposure. This book is among the first of its kind to include detailed risk estimates for cancer incidence in addition to cancer mortality. BEIR VII offers a full review of the available biological, biophysical, and epidemiological literature since the last BEIR report on the subject and develops the most up-to-date and comprehensive risk estimates for cancer and other health effects from exposure to low-level ionizing radiation.
An increasingly aging population will add to the number of individuals suffering from amyloid. Protein Misfolding Diseases provides a systematic overview of the current and emerging therapies for these types of protein misfolding diseases, including Alzheimer's, Parkinson's, and Mad Cow. The book emphasizes therapeutics in an amyloid disease context to help students, faculty, scientific researchers, and doctors working with protein misfolding diseases bridge the gap between basic science and pharmaceutical applications to protein misfolding disease.