Protein Structure And Diseases

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Protein Structure

Author : Max F. Perutz
Publisher : Unknown
Page : 326 pages
File Size : 42,6 Mb
Release : 1992
Category : Proteins
ISBN : 0716723107

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Protein Structure by Max F. Perutz Pdf

Protein Misfolding, Aggregation and Conformational Diseases

Author : Vladimir N. Uversky,Anthony Fink
Publisher : Springer Science & Business Media
Page : 450 pages
File Size : 52,8 Mb
Release : 2007-11-24
Category : Science
ISBN : 9780387259192

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Protein Misfolding, Aggregation and Conformational Diseases by Vladimir N. Uversky,Anthony Fink Pdf

Research indicates that most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. This is the first book to discuss significant achievements in protein structure-function relationships in biochemistry, molecular biology and molecular medicine. The authors summarize recent progress in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders.

Protein Structure and Diseases

Author : Rossen Donev
Publisher : Academic Press
Page : 322 pages
File Size : 54,6 Mb
Release : 2011-05-27
Category : Medical
ISBN : 9780123812629

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Protein Structure and Diseases by Rossen Donev Pdf

Structural genomics is the systematic determination of 3D structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome. While most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale. Examines the three dimensional structure of all proteins of a given organism, by experimental methods such as X-ray crystallography and NMR spectroscopy Looks at structural genomics as a foundation of drug discovery as discovering new medicines is becoming more challenging and the pharmaceutical industry is looking to new technologies to help in this mission

Fundamentals of Protein Structure and Function

Author : Engelbert Buxbaum
Publisher : Springer
Page : 521 pages
File Size : 41,8 Mb
Release : 2015-11-27
Category : Science
ISBN : 9783319199207

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Fundamentals of Protein Structure and Function by Engelbert Buxbaum Pdf

This book serves as an introduction to protein structure and function. Starting with their makeup from simple building blocks, called amino acids, the 3-dimensional structure of proteins is explained. This leads to a discussion how misfolding of proteins causes diseases like cancer, various encephalopathies, or diabetes. Enzymology and modern concepts of enzyme kinetics are then introduced, taking into account the physiological, pharmacological and medical significance of this often neglected topic. This is followed by thorough coverage of hæmoglobin and myoglobin, immunoproteins, motor proteins and movement, cell-cell interactions, molecular chaperones and chaperonins, transport of proteins to various cell compartments and solute transport across biological membranes. Proteins in the laboratory are also covered, including a detailed description of the purification and determination of proteins, as well as their characterisation for size and shape, structure and molecular interactions. The book emphasises the link between protein structure, physiological function and medical significance. This book can be used for graduate and advanced undergraduate classes covering protein structure and function and as an introductory text for researchers in protein biochemistry, molecular and cell biology, chemistry, biophysics, biomedicine and related courses. About the author: Dr. Buxbaum is a biochemist with interest in enzymology and protein science. He has been working on the biochemistry of membrane transport proteins for nearly thirty years and has taught courses in biochemistry and biomedicine at several universities.

Molecular Biology of The Cell

Author : Bruce Alberts
Publisher : Unknown
Page : 0 pages
File Size : 44,7 Mb
Release : 2002
Category : Cytology
ISBN : 0815332181

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Molecular Biology of The Cell by Bruce Alberts Pdf

Frontiers in Protein Structure, Function, and Dynamics

Author : Dev Bukhsh Singh,Timir Tripathi
Publisher : Springer Nature
Page : 458 pages
File Size : 54,5 Mb
Release : 2020-07-02
Category : Science
ISBN : 9789811555305

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Frontiers in Protein Structure, Function, and Dynamics by Dev Bukhsh Singh,Timir Tripathi Pdf

This book discusses a broad range of basic and advanced topics in the field of protein structure, function, folding, flexibility, and dynamics. Starting with a basic introduction to protein purification, estimation, storage, and its effect on the protein structure, function, and dynamics, it also discusses various experimental and computational structure determination approaches; the importance of molecular interactions and water in protein stability, folding and dynamics; kinetic and thermodynamic parameters associated with protein-ligand binding; single molecule techniques and their applications in studying protein folding and aggregation; protein quality control; the role of amino acid sequence in protein aggregation; muscarinic acetylcholine receptors, antimuscarinic drugs, and their clinical significances. Further, the book explains the current understanding on the therapeutic importance of the enzyme dopamine beta hydroxylase; structural dynamics and motions in molecular motors; role of cathepsins in controlling degradation of extracellular matrix during disease states; and the important structure-function relationship of iron-binding proteins, ferritins. Overall, the book is an important guide and a comprehensive resource for understanding protein structure, function, dynamics, and interaction.

Protein Misfolding Diseases

Author : Marina Ramirez-Alvarado,Jeffery W. Kelly,Christopher M. Dobson
Publisher : John Wiley & Sons
Page : 1311 pages
File Size : 54,5 Mb
Release : 2010-12-01
Category : Science
ISBN : 9781118031810

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Protein Misfolding Diseases by Marina Ramirez-Alvarado,Jeffery W. Kelly,Christopher M. Dobson Pdf

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.

Homocysteine in Protein Structure/Function and Human Disease

Author : Hieronim Jakubowski
Publisher : Springer Science & Business Media
Page : 175 pages
File Size : 43,6 Mb
Release : 2013-06-20
Category : Science
ISBN : 9783709114100

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Homocysteine in Protein Structure/Function and Human Disease by Hieronim Jakubowski Pdf

Excess of homocysteine, a product of the metabolism of the essential amino acid methionine, is associated with poor health, is linked to heart and brain diseases in general human populations, and accelerates mortality in heart disease patients. Neurological and cardiovascular abnormalities occur in patients with severe genetic hyperhomocysteinemia and lead to premature death due to vascular complications. Although it is considered a non-protein amino acid, studies over the past dozen years have discovered mechanisms by which homocysteine becomes a component of proteins. Homocysteine-containing proteins lose their normal biological function and become auto-immunogenic and pro-thrombotic. In this book, the author, a pioneer and a leading contributor to the field, describes up-to date studies of the biological chemistry of homocysteine-containing proteins, as well as pathological consequences and clinical implications of their formation. This is a comprehensive account of the broad range of basic science and medical implications of homocysteine-containing proteins for health and disease. ​

Molecular Dynamics Analyses of Prion Protein Structures

Author : Jiapu Zhang
Publisher : Springer
Page : 375 pages
File Size : 46,6 Mb
Release : 2018-07-20
Category : Science
ISBN : 9789811088155

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Molecular Dynamics Analyses of Prion Protein Structures by Jiapu Zhang Pdf

Unlike bacteria and viruses, which are based on DNA and RNA, prions are unique as disease-causing agents since they are misfolded proteins. Prion diseases are called "protein structural conformational” diseases. This monograph is the book on molecular dynamics (MD) simulations nearly for all the known normal prion protein (PrPC) PDB entries in the Protein Data Bank (PDB) and associations. Pig is a species that is largely resistant to prions, and chicken, turtles, frogs are species resisting prion infection too; firstly, this book will address all PrP strong immunity species (such as rabbits, dogs, horses, water buffaloes, pigs, chicken, turtles, frogs), compared with high susceptibility species. Other PrP models and doppel models are also MD studied in this book. Secondly, all the mutants of mouse PrP and human PrP are well studied by this book. Mouse mutations in the β2-α2 loop and the C-terminal will bring clear structures with highly and clearly ordered loop structures. Human mutations will cause prion diseases such as Creutzfeldt-Jakob diseases (CJDs), Gerstmann-Sträussler-Scheinker (GSS) syndrome, fatal familial insomnia (FFI), etc. Deep MD analyses of mouse and human mutants are done in this book. Thirdly, PrP binding with antibodies/compounds etc. is well MD studied in this book. The informatics of potential antiprion drugs known will be revealed. Lastly, cross-β structure PrP peptides are well studied. This book is ideal for practical computing staff in the fields of computational physics, computational biology, computational chemistry, biomedicine, bioinformatics, cheminformatics, materials, applied mathematics and theoretical physics, information technology, operations research, biostatistics, etc. As an accessible introduction to these fields, this book is also ideal as a teaching material for students.

Protein Dysfunction in Human Genetic Disease

Author : D.M. Swallow,Y.H. Edwards
Publisher : Unknown
Page : 272 pages
File Size : 53,8 Mb
Release : 1997-01-01
Category : Medical
ISBN : 0122204441

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Protein Dysfunction in Human Genetic Disease by D.M. Swallow,Y.H. Edwards Pdf

Comprehensive coverage of human genetic disease mechanisms. Describes important models of protein dysfunction in human genetic disease. Many of our genes have now been identified and sequenced, and genetic disease can be described in terms of DNA sequence. Research endeavors are now aimed at understanding the structure and function of the protein products of disease genes. Analysis of protein malfunctions in genetic diseases provides an invaluable approach to this undertaking. Protein Dysfunction in Human Genetic Disease focuses on DNA mutations which give rise to abnormalities in protein structure and function. Authoritative reviews of specific proteins or protein complexes illustrate how mutations which interfere with protein-protein interactions, ligand and substrate binding, secretion, membrane assembly, intracellular localization and transport, or post-translational processing underlie the disease process. Genetic and biochemical perspectives are both emphasized in Protein Dysfunction in Human Genetic Disease. The chapters provide general models for the guidance of researchers who are looking for a function for their disease protein or are seeking to explain a clinical phenotype. This book will also benefit final year and postgraduate students of genetics and biochemistry, and interest all who are curious about protein function. Key Features * Comprehensive coverage of human genetic disease mechanisms * Describes important models of protein dysfunction in human genetic disease

Protein Misfolding, Aggregation and Conformational Diseases

Author : Vladimir N. Uversky,Anthony Fink
Publisher : Springer Science & Business Media
Page : 538 pages
File Size : 47,9 Mb
Release : 2007-05-26
Category : Medical
ISBN : 9780387365343

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Protein Misfolding, Aggregation and Conformational Diseases by Vladimir N. Uversky,Anthony Fink Pdf

The second volume continues to fill the gap in protein review and protocol literature. It does this while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.

Models, Molecules and Mechanisms in Biogerontology

Author : Pramod C. Rath
Publisher : Springer
Page : 0 pages
File Size : 44,7 Mb
Release : 2020-06-27
Category : Medical
ISBN : 9813290048

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Models, Molecules and Mechanisms in Biogerontology by Pramod C. Rath Pdf

The book deals with basic cellular and molecular mechanisms associated with aging. It comprehensively describes the important genetic, epigenetic, biochemical and metabolic regulations during aging, as well as some important age-related diseases.The book is divided into four major sections for easy understanding. It takes the readers through the various aspects of aging in a story-like manner. Certain interventions for healthy aging such as dietary restriction, regular exercise and maintaining a balanced and peaceful life-style are also suggested by the experts. The book would be a companion for both beginners, as well as established researchers in the field. It would be useful for science education, research, clinical approach and policy making.

On protein structure, function and modularity from an evolutionary perspective

Author : Robert Pilstål
Publisher : Linköping University Electronic Press
Page : 77 pages
File Size : 52,7 Mb
Release : 2018-05-31
Category : Electronic
ISBN : 9789176853474

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On protein structure, function and modularity from an evolutionary perspective by Robert Pilstål Pdf

We are compounded entities, given life by a complex molecular machinery. When studying these molecules we have to make sense of a diverse set of dynamical nanostructures with wast and intricate patterns of interactions. Protein polymers is one of the major groups of building blocks of such nanostructures which fold up into more or less distinct three dimensional structures. Due to their shape, dynamics and chemical properties proteins are able to perform a plethora of specific functions essential to all known cellular lifeforms. The connection between protein sequence, translated into protein structure and in the continuation into protein function is well accepted but poorly understood. Malfunction in the process of protein folding is known to be implicated in natural aging, cancer and degenerative diseases such as Alzheimer's. Protein folds are described hierarchically by structural ontologies such as SCOP, CATH and Pfam all which has yet to succeed in deciphering the natural language of protein function. These paradigmatic views centered on protein structure fail to describe more mutable entities, such as intrinsically disordered proteins (IDPs) which lack a clear defined structure. As of 2012, about two thirds of cancer patients was predicted to survive past 5 years of diagnosis. Despite this, about a third do not survive and numerous of successfully treated patients suffer from secondary conditions due to chemotherapy, surgery and the like. In order to handle cancer more efficiently we have to better understand the underlying molecular mechanisms. Elusive to standard methods of investigation, IDPs have a central role in pathology; dysfunction in IDPs are key factors in cellular system failures such as cancer, as many IDPs are hub regulators for major cell functions. These IDPs carry short conserved functional boxes, that are not described by known ontologies, which suggests the existence of a smaller entity. In an investigation of a pair of such boxes of c-MYC, a plausible structural model of its interacting with Pin1 emerged, but such a model still leaves the observer with a puzzle of understanding the actual function of that interaction. If the protein is represented as a graph and modeled as the interaction patterns instead of as a structural entity, another picture emerges. As a graph, there is a parable from that of the boxes of IDPs, to that of sectors of allosterically connected residues and the theory of foldons and folding units. Such a description is also useful in deciphering the implications of specific mutations. In order to render a functional description feasible for both structured and disordered proteins, there is a need of a model separate from form and structure. Realized as protein primes, patterns of interaction, which has a specific function that can be defined as prime interactions and context. With function defined as interactions, it might be possible that the discussion of proteins and their mechanisms is thereby simplified to the point rendering protein structural determination merely supplementary to understanding protein function. Människan byggs upp av celler, de i sin tur består av än mindre beståndsdelar; livets molekyler. Dessa fungerar som mekaniska byggstenar, likt maskiner och robotar som sliter vid fabrikens band; envar utförandes en absolut nödvändig funktion för cellens, och hela kroppens, fortsatta överlevnad. De av livets molekyler som beskrivs centralt i den här avhandling är proteiner, vilka i sin tur består utav en lång kedja, med olika typer av länkar, som likt garn lindar upp sig i ett nystan av en (mer eller mindre...) bestämd struktur som avgör dess roll och funktion i cellen. Intrinsiellt oordnade proteiner (IDP) går emot denna enkla åskådning; de är proteiner som saknar struktur och beter sig mer likt spaghetti i vatten än en maskin. IDP är ändå funktionella och bär på centrala roller i cellens maskineri; exempel är oncoproteinet c-Myc som agerar "gaspedal" för cellen - fel i c-Myc's funktion leder till att cellerna löper amok, delar sig hejdlöst och vi får cancer. Man har upptäckt att c-Myc har en ombytlig struktur vi inte kan se; studier av punktvisa förändringar, mutationer, i kedjan av byggstenar hos c-Myc visar att många länkar har viktiga roller i funktionen. Detta ger oss bättre förståelse om cancer men samtidigt är laboratoriearbetet både komplicerat och dyrt; här kan evolutionen vägleda oss och avslöja hemligheterna snabbare. Molekylär evolution studeras genom att beräkna variation i proteinkedjan mellan besläktade arter som finns lagrade i databaser; detta visar snabbt, via nätverksanalys och grafteori, vilka delar av proteinet som är centrala och kopplade till varandra av nödvändighet för artens fortlevnad. På så vis hjälper evolutionen oss att förstå proteinfunktioner via modeller baserade på proteinernas interaktioner snarare än deras struktur. Samma modeller kan nyttjas för att förstå dynamiska förlopp och skillnader mellan normala och patologiska varianter av proteiner; mutationer kan uppstå i vår arvsmassa som kan leda till sjukdom. Genom analys av proteinernas kopplingsnätverk i grafmodellerna kan man bättre förutsäga vilka mutationer som är farligare än andra. Dessutom har det visat sig att en sådan representation kan ge bättre förståelse för den normala funktionen hos ett protein än vad en proteinstruktur kan. Här introduceras även konceptet proteinprimärer, vilket är en abstrakt representation av proteiner centrerad på deras interaktiva mönster, snarare än på partikulär form och struktur. Det är en förhoppning att en sådan representation skall förenkla diskussionen anbelangande proteinfunktion så till den grad att strukturbestämmelse av proteiner, som är en mycket kostsam och tidskrävande process, till viss mån kan anses vara sekundär i betydelse jämfört med funktionellt modellerande baserat på evolutionära data extraherade ur våra sekvensdatabaser.

Protein Misfolding, Aggregation and Conformational Diseases

Author : Vladimir N. Uversky,Anthony Fink
Publisher : Springer
Page : 538 pages
File Size : 40,9 Mb
Release : 2007-02-21
Category : Medical
ISBN : 038736529X

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Protein Misfolding, Aggregation and Conformational Diseases by Vladimir N. Uversky,Anthony Fink Pdf

The second volume continues to fill the gap in protein review and protocol literature. It does this while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.

Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A

Author : Anonim
Publisher : Academic Press
Page : 0 pages
File Size : 55,5 Mb
Release : 2019-09-12
Category : Science
ISBN : 012816851X

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Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A by Anonim Pdf

"Dancing protein clouds: Intrinsically disordered proteins in the norm and pathology" represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins. Topics in this update include structural and functional characterization of several important intrinsically disordered proteins, such as 14-3-3 proteins and their partners, as well as proteins from muscle sarcomere; representation of intrinsic disorder-related concept of protein structure-function continuum; discussion of the role of intrinsic disorder in phenotypic switching; consideration of the role of intrinsically disordered proteins in the pathogenesis of neurodegenerative diseases and cancer; discussion of the roles of intrinsic disorder in functional amyloids; demonstration of the usefulness of the analysis of translational diffusion of unfolded and intrinsically disordered proteins; consideration of various computational tools for evaluation of functions of intrinsically disordered regions; and discussion of the role of shear stress in the amyloid formation of intrinsically disordered regions in the brain.