Water in Biological and Chemical Processes PDF Download
Are you looking for read ebook online? Search for your book and save it on your Kindle device, PC, phones or tablets. Download Water in Biological and Chemical Processes PDF full book. Access full book title Water in Biological and Chemical Processes by Biman Bagchi. Download full books in PDF and EPUB format.
Author: Biman Bagchi
Publisher: Cambridge University Press
ISBN: 1107037298
Category : Medical
Languages : en
Pages : 383
Get Book Here
Book Description
A unified overview of the dynamical properties of water and its unique and diverse role in biological and chemical processes.
Author: Biman Bagchi
Publisher: Cambridge University Press
ISBN: 1107037298
Category : Medical
Languages : en
Pages : 383
Get Book Here
Book Description
A unified overview of the dynamical properties of water and its unique and diverse role in biological and chemical processes.
Author: Masayoshi Nakasako
Publisher: Springer Nature
ISBN: 4431569197
Category : Science
Languages : en
Pages : 321
Get Book Here
Book Description
This book describes hydration structures of proteins by combining experimental results with theoretical considerations. It is designed to introduce graduate students and researchers to microscopic views of the interactions between water and biological macromolecules and to provide them with an overview of the field. Topics on protein hydration from the past 25 years are examined, most of which involve crystallography, fluorescence measurements, and molecular dynamics simulations. In X-ray crystallography and molecular dynamics simulations, recent advances have accelerated the study of hydration structures over the entire surface of proteins. Experimentally, crystal structure analysis at cryogenic temperatures is advantageous in terms of visualizing the positions of hydration water molecules on the surfaces of proteins in their frozen-hydrated crystals. A set of massive data regarding hydration sites on protein surfaces provides an appropriate basis, enabling us to identify statistically significant trends in geometrical characteristics. Trajectories obtained from molecular dynamics simulations illustrate the motion of water molecules in the vicinity of protein surfaces at sufficiently high spatial and temporal resolution to study the influences of hydration on protein motion. Together with the results and implications of these studies, the physical principles of the measurement and simulation of protein hydration are briefly summarized at an undergraduate level. Further, the author presents recent results from statistical approaches to characterizing hydrogen-bond geometry in local hydration structures of proteins. The book equips readers to better understand the structures and modes of interaction at the interface between water and proteins. Referred to as “hydration structures”, they are the subject of much discussion, as they may help to answer the question of why water is indispensable for life at the molecular and atomic level.
Author: Bernard Pullman
Publisher: Springer
ISBN:
Category : Science
Languages : en
Pages : 588
Get Book Here
Book Description
Proceedings of the 14th Jerusalem Symposium on Quantum Chemistry and Biochemistry, Jerusalem, Israel, April 13-16, 1981
Author: Gertz I. Likhtenshtein
Publisher: Springer Nature
ISBN: 3030825035
Category : Science
Languages : en
Pages : 523
Get Book Here
Book Description
This book embraces all physiochemical aspects of the structure and molecular dynamics of water, focusing on its role in biological objects, e.g. living cells and tissue, and in the formation of functionally active structures of biological molecules and their ensembles. Water is the single most abundant chemical found in all living things. It offers a detailed look into the latest modern physical methods for studying the molecular structure and dynamics of the water and provides a critical analysis of the existing literature data on the properties of water in biological objects. Water as a chemical reagent and as a medium for the formation of conditions for enzymatic catalysis is a core focus of this book. Although well suited for active researchers, the book as a whole, as well as each chapter on its own, can be used as fundamental reference material for graduate and undergraduate students throughout chemistry, physics, biophysics and biomedicine.
Author: Vladimir A. Sirotkin
Publisher:
ISBN: 9781536160208
Category : Proteins
Languages : en
Pages : 0
Get Book Here
Book Description
This book describes the basic principles of a novel methodology to investigate the preferential hydration and solvation of proteins in ternary protein-water-organic solvent systems. Protein-water interactions are well-known to play a critical role in determining the function, structure, and stability of protein macromolecules. Elucidation of the processes occurring upon protein hydration in the presence of third component (organic solvents, salts, urea) is essential in a wide range of biophysical, biomedical, and biotechnological applications. In particular, there are many advantages in employing water-poor organic solvents, including the suppression of undesirable side reactions caused by water, the biocatalysis of reversed hydrolytic reactions (transesterification, peptide synthesis), or increased thermostability. Distinct intermediate protein states induced by organic solvents may be responsible for numerous neurodegenerative diseases (Alzheimer's disease, Parkinson's disease, and Huntington's disease). However, the manner in which organic solvents increase/decrease the thermal stability, induce/reduce the extent of denaturation, and stabilize/destabilize the partially folded conformations of proteins (amyloid fibrils and molten globules) is an intricate function of water content in organic liquids. Preferential hydration/solvation is an effective method for revealing the mechanism of the protein stabilization or denaturation. When a protein interacts with a binary water-organic solvent mixture, the three components do not equally mix. Water or organic solvent molecules exist preferentially in the protein's solvation shell. This difference between the solvation shell and bulk solvent in the solvent components has been termed preferential solvation. Preferential solvation is a thermodynamic quantity that describes the protein surface occupancy by the water and cosolvent molecules. This is associated with the actual numbers of water/cosolvent molecules that are in contact with the protein's surface. It was also found that the protein destabilization is directly associated with the preferential binding of the denaturant molecules to specific protein groups.The aim of our study is to monitor the preferential solvation and preferential hydration of the protein macromolecules at low, intermediate, and high water content in organic solvents at 25 oC. Our approach is based on the simultaneous measurements of the absolute values of the water and organic solvent sorption. The preferential solvation/hydration parameters were calculated using the water and organic solvent sorption values. The preferential solvation/hydration parameters were compared with the corresponding changes in the protein structure that transpire regarding the interaction of the protein with organic solvent and water molecules. The effect of organic solvent on the protein structure was investigated by FTIR (Fourier Transform Infrared) spectroscopy.
Author: E. Anibal Disalvo
Publisher: Springer
ISBN: 3319190601
Category : Science
Languages : en
Pages : 295
Get Book Here
Book Description
This book is about the importance of water in determining the structure, stability and responsive behavior of biological membranes. Water confers to lipid membranes unique features in terms of surface and mechanical properties. The analysis of the hydration forces, plasticiser effects, controlled hydration, formation of microdomains of confined water suggests that water is an active constituent in a water-lipid system. The chapters describe water organization at the lipid membrane–water interphase, the water penetration, the long range water structure in the presence of lipid membranes by means of X-ray and neutron scattering, general polarization, fluorescent probes, ATR-FTIR and near infrared spectroscopies, piezo electric methods, computer simulation and surface thermodynamics. Permeation, percolation, osmotic stress, polarization, protrusion, sorption, hydrophobicity, density fluctuations are treated in detail in self-assembled bilayers. Studies in lipid monolayers show the correlation of surface pressure with water activity and its role in peptide and enzyme interactions. The book concludes with a discussion on anhydrobiosis and the effect of water replacement in microdomains and its consequence for cell function. New definitions of lipid/water interphases consider water not only as a structural-making solvent but as a mediator in signalling metabolic activity, modulating protein insertion and enzymatic activity, triggering oscillatory reactions and functioning of membrane bound receptors. Since these effects occur at the molecular level, membrane hydration appears fundamental to understand the behavior of nano systems and confined environments mimicking biological systems. These insights in structural, thermodynamical and mechanical water properties give a base for new paradigms in membrane structure and function for those interested in biophysics, physical chemistry, biology, bio and nano medicine, biochemistry, biotechnology and nano sciences searching for biotechnological inputs in human health, food industry, plant growing and energy conversion.
Author: Kurt Wuthrich
Publisher: World Scientific
ISBN: 9814500496
Category : Science
Languages : en
Pages : 760
Get Book Here
Book Description
The volume presents a survey of the research by Kurt Wüthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.
Author: M.C. Bellissent-Funel
Publisher: Springer Science & Business Media
ISBN: 9401583323
Category : Science
Languages : en
Pages : 564
Get Book Here
Book Description
The almost universal presence of water in our everyday lives and the very `common' nature of its presence and properties possibly deflects attention from the fact that it has a number of very unusual characteristics which, furthermore, are found to be extremely sensitive to physical parameters, chemical environment and other influences. Hydrogen-bonding effects, too, are not restricted to water, so it is necessary to investigate other systems as well, in order to understand the characteristics in a wider context. Hydrogen Bond Networks reflects the diversity and relevance of water in subjects ranging from the fundamentals of condensed matter physics, through aspects of chemical reactivity to structure and function in biological systems.
Author: Masayoshi Nakasako
Publisher:
ISBN: 9784431569183
Category :
Languages : en
Pages : 0
Get Book Here
Book Description
This book describes hydration structures of proteins by combining experimental results with theoretical considerations. It is designed to introduce graduate students and researchers to microscopic views of the interactions between water and biological macromolecules and to provide them with an overview of the field. Topics on protein hydration from the past 25 years are examined, most of which involve crystallography, fluorescence measurements, and molecular dynamics simulations. In X-ray crystallography and molecular dynamics simulations, recent advances have accelerated the study of hydration structures over the entire surface of proteins. Experimentally, crystal structure analysis at cryogenic temperatures is advantageous in terms of visualizing the positions of hydration water molecules on the surfaces of proteins in their frozen-hydrated crystals. A set of massive data regarding hydration sites on protein surfaces provides an appropriate basis, enabling us to identify statistically significant trends in geometrical characteristics. Trajectories obtained from molecular dynamics simulations illustrate the motion of water molecules in the vicinity of protein surfaces at sufficiently high spatial and temporal resolution to study the influences of hydration on protein motion. Together with the results and implications of these studies, the physical principles of the measurement and simulation of protein hydration are briefly summarized at an undergraduate level. Further, the author presents recent results from statistical approaches to characterizing hydrogen-bond geometry in local hydration structures of proteins. The book equips readers to better understand the structures and modes of interaction at the interface between water and proteins. Referred to as "hydration structures", they are the subject of much discussion, as they may help to answer the question of why water is indispensable for life at the molecular and atomic level.
Author: Roger Gregory
Publisher: CRC Press
ISBN: 1040282512
Category : Science
Languages : en
Pages : 596
Get Book Here
Book Description
This work covers advances in the interactions of proteins with their solvent environment and provides fundamental physical information useful for the application of proteins in biotechnology and industrial processes. It discusses in detail structure, dynamic and thermodynamic aspects of protein hydration, as well as proteins in aqueous and organic solvents as they relate to protein function, stability and folding.
