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Author: James D. Gunton
Publisher: Cambridge University Press
ISBN: 9781107424272
Category : Science
Languages : en
Pages : 394
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Book Description
The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.
Author: James D. Gunton
Publisher: Cambridge University Press
ISBN: 9780521851213
Category : Science
Languages : en
Pages : 376
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Book Description
The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.
Author: James D. Gunton
Publisher: Cambridge University Press
ISBN: 9781107424272
Category : Science
Languages : en
Pages : 394
Get Book Here
Book Description
The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.
Author:
Publisher: Academic Press
ISBN: 0128122528
Category : Science
Languages : en
Pages : 322
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Book Description
Early Stage Protein Misfolding and Amyloid Aggregation, Volume 329, the latest in the International Review of Cell and Molecular Biology series presents comprehensive reviews and current advances in cell and molecular biology, including articles that address the structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. The series has a worldwide readership and maintains a high standard by publishing invited articles on important and timely topics as authored by prominent cell and molecular biologists. Provides comprehensive reviews and current advances Presents a wide range of perspectives on specific subjects Includes valuable reference material for advanced undergraduates, graduate students, and professional scientists
Author: Ying Wang
Publisher:
ISBN:
Category : Condensation
Languages : en
Pages :
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Book Description
The formation of protein condensed phases (e.g., aggregates, gels and crystals) from aqueous solutions is important in materials science, biology, medicine and biotechnology. However this process is not well-understood and physicochemical studies on protein condensation are fundamental for all the above areas. Protein condensation induced in the presence macromolecular additives is known as macromolecular crowding. Although this process is not well-understood, it is believed that the main action of these additives is to enhance protein condensation by depletion interactions related to the size of macromolecules. Polyethylene glycol (PEG), a hydrophilic nonionic polymer, is one of the most widely used macromolecular-crowding agents. Upon the addition of PEG with an average molecular weight of 1450 g/mol (PEG1450) to bovine serum albumin (BSA) aqueous solutions, protein condensation into oil-like spherical droplets is observed by lowering temperature. This phenomenon is related to liquid-liquid phase separation (LLPS). To investigate the crowding effect of PEG on protein condensation, two thermodynamically independent properties of the LLPS phase boundary were experimentally characterized: (1) the effect of PEG1450 concentration on the LLPS temperature, (2) BSA/PEG1450 partitioning in the two liquid coexisting phases. A thermodynamic perturbation theory, which includes one parameter describing depletion interactions, was used to examine our experimental results. It was found that both independent properties of the phase boundary could be quantitatively described by the same value of the depletion-interaction parameter. However, the depletion-interaction parameter determined from our LLPS experiments was found to be significantly different from that theoretically obtained from the molecular size of BSA and PEG1450 by treating PEG as an ideal chain. The non-ideal behavior of the PEG chain was hypothesized as the main reason for the observed discrepancy. Thus, a more realistic model for the PEG chain was introduced. Monte-Carlo simulations were then performed to calculate novel values of the depletion-interaction parameter from the size of BSA and PEG1450. It is then shown that our new model for PEG chains significantly improves the agreement between experimental results and theory. The role of protein oligomerization on protein condensation was also investigated. It is shown that LLPS of protein aqueous solutions can be isothermally induced by protein oligomerization. For BSA and lysozyme as protein models, protein oligomerization in the presence of glutaraldehyde as a chemical cross-linker can evolve either towards the formation of cross-linked protein condensed droplets or macroscopic amorphous aggregation, depending on the LLPS properties of the protein monomer. Finally, laccase condensation from aqueous solutions was investigated. Laccase is an enzyme used in the petroleum, paper and food industry. The thermodynamic behavior of laccase condensation and the morphology of laccase condensed phases was observed to strongly depend on the nature of the additive (PEG or (NH4)2SO4). Interestingly, laccase condensation could be also induced by using liquid-liquid interfaces. At low enzyme concentrations, it is shown that laccase condensation can be driven by BSA-laccase cross-linking and BSA condensation. This has produced catalytically-active aggregates. The reported preliminary results on laccase provide the basis for more systematic experimental and theoretical investigations on this system.
Author: Robert Henry Aders Plimmer
Publisher:
ISBN:
Category : Proteins
Languages : en
Pages : 88
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Book Description
Author: Weibo Cai
Publisher: BoD – Books on Demand
ISBN: 9535103970
Category : Science
Languages : en
Pages : 488
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Book Description
Proteins are indispensable players in virtually all biological events. The functions of proteins are coordinated through intricate regulatory networks of transient protein-protein interactions (PPIs). To predict and/or study PPIs, a wide variety of techniques have been developed over the last several decades. Many in vitro and in vivo assays have been implemented to explore the mechanism of these ubiquitous interactions. However, despite significant advances in these experimental approaches, many limitations exist such as false-positives/false-negatives, difficulty in obtaining crystal structures of proteins, challenges in the detection of transient PPI, among others. To overcome these limitations, many computational approaches have been developed which are becoming increasingly widely used to facilitate the investigation of PPIs. This book has gathered an ensemble of experts in the field, in 22 chapters, which have been broadly categorized into Computational Approaches, Experimental Approaches, and Others.
Author: Jay A. Glasel
Publisher: Academic Press
ISBN: 0080534988
Category : Science
Languages : en
Pages : 528
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Book Description
The first of its kind, Introduction to Biophysical Methods for Protein and Nucleic Acid Research serves as a text for the experienced researcher and student requiring an introduction to the field. Each chapter presents a description of the physical basis of the method, the type of information that may be obtained with the method, how data should be analyzed and interpreted and, where appropriate, practical tips about procedures and equipment. Key Features* Modern Use of Mass Spectroscopy* NMR Spectroscopy* Molecular Modeling and Graphics* Macintosh and DOS/Windows 3.x disks
Author: Ivan Cameron
Publisher: Elsevier
ISBN: 0323154123
Category : Science
Languages : en
Pages : 363
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Book Description
Acidic Proteins of the Nucleus focuses on the functional role of acidic nuclear proteins in differential gene expression. Historically, these proteins are referred to as acidic in nature because they are insoluble in dilute mineral acids and their amino acid composition shows a preponderance of acidic over basic amino acid residues. After an introduction to DNA-binding proteins and transcriptional control in prokaryotic and eukaryotic systems, the subsequent chapters describe various approaches for isolating, separating, and characterizing acidic nuclear proteins. The core chapters specifically cover the isolation, fractionation, and characterization of acidic nuclear phosphoproteins, and the role of these proteins in cell proliferation, cell differentiation, and cell cycle. The last two chapters address the role of acidic nuclear protein in binding steroid hormones and in gene regulation. Each chapter contains some previously unpublished work and provides recommendations for future research. This book will be a good reference background for researchers of acidic nuclear proteins.
Author: Andrzej Stanisław Cieplak
Publisher: Springer Nature
ISBN: 1071625977
Category : Science
Languages : en
Pages : 673
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Book Description
The volume details techniques, methods, and conceptual developments to further the study of protein aggregation with emphasis on the pleiomorphic proteins implicated in etiology of neurodegeneration. Chapters guide readers through in vitro and in vivo studies of fibrillization and liquid-liquid phase separation processes, and offer a comprehensive account of the state-of-art of structural studies of protein aggregation. Written in the format of the highly successful Methods in Molecular Biology series, each chapter includes an introduction to the topic, lists necessary materials and reagents, includes tips on troubleshooting and known pitfalls, and step-by-step, readily reproducible protocols. Authoritative and cutting-edge, Protein Aggregation: Methods and Protocols aims to be useful and practical guide to new researchers and experts looking to expand their knowledge.
Author: Bruce Alberts
Publisher:
ISBN: 9780815332183
Category : Cytology
Languages : en
Pages : 0
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Book Description
