Preferential Solvation and Hydration of Proteins in Water-organic Mixtures:
Preferential Solvation and Hydration of Proteins in Water-organic Mixtures:

Author: Vladimir A. Sirotkin

Publisher:

Published: 2019

Total Pages: 0

ISBN-13: 9781536160208

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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.

Protein-Solvent Interactions
Protein-Solvent Interactions

Author: Roger Gregory

Publisher: CRC Press

Published: 2024-11-01

Total Pages: 596

ISBN-13: 1040282512

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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.

Water in Biological and Chemical Processes
Water in Biological and Chemical Processes

Author: Biman Bagchi

Publisher: Cambridge University Press

Published: 2013-11-14

Total Pages: 383

ISBN-13: 1107037298

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A unified overview of the dynamical properties of water and its unique and diverse role in biological and chemical processes.

Solvents and Solvent Effects in Organic Chemistry
Solvents and Solvent Effects in Organic Chemistry

Author: Christian Reichardt

Publisher: John Wiley & Sons

Published: 2011-08-04

Total Pages: 722

ISBN-13: 3527642137

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Now in its 4th edition, this book remains the ultimate reference for all questions regarding solvents and solvent effects in organic chemistry. Retaining its proven concept, there is no other book which covers the subject in so much depth, the handbook is completely updated and contains 15% more content, including new chapters on "Solvents and Green chemistry", "Classification of Solvents by their Environmental Impact", and "Ionic Liquids". An essential part of every organic chemist's library.

Modern Magnetic Resonance
Modern Magnetic Resonance

Author: Graham A. Webb

Publisher: Springer Science & Business Media

Published: 2007-05-26

Total Pages: 1889

ISBN-13: 1402039107

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A comprehensive collection of the applications of Nuclear Magnetic Resonance (NMR), Magnetic Resonance Imaging (MRI) and Electron-Spin Resonance (ESR). Covers the wide ranging disciplines in which these techniques are used: * Chemistry; * Biological Sciences; * Pharmaceutical Sciences; * Medical uses; * Marine Science; * Materials Science; * Food Science. Illustrates many techniques through the applications described, e.g.: * High resolution solid and liquid state NMR; * Low resolution NMR, especially important in food science; * Solution State NMR, especially important in pharmaceutical sciences; * Magnetic Resonance Imaging, especially important for medical uses; * Electron Spin Resonance, especially important for spin-labelling in food, marine and medical studies.

Thermodynamics of Solutions
Thermodynamics of Solutions

Author: Eli Ruckenstein

Publisher: Springer Science & Business Media

Published: 2009-06-17

Total Pages: 349

ISBN-13: 1441904409

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This book consists of a number of papers regarding the thermodynamics and structure of multicomponent systems that we have published during the last decade. Even though they involve different topics and different systems, they have something in common which can be considered as the “signature” of the present book. First, these papers are concerned with “difficult” or very nonideal systems, i. e. systems with very strong interactions (e. g. , hyd- gen bonding) between components or systems with large differences in the partial molar v- umes of the components (e. g. , the aqueous solutions of proteins), or systems that are far from “normal” conditions (e. g. , critical or near-critical mixtures). Second, the conventional th- modynamic methods are not sufficient for the accurate treatment of these mixtures. Last but not least, these systems are of interest for the pharmaceutical, biomedical, and related ind- tries. In order to meet the thermodynamic challenges involved in these complex mixtures, we employed a variety of traditional methods but also new methods, such as the fluctuation t- ory of Kirkwood and Buff and ab initio quantum mechanical techniques. The Kirkwood-Buff (KB) theory is a rigorous formalism which is free of any of the - proximations usually used in the thermodynamic treatment of multicomponent systems. This theory appears to be very fruitful when applied to the above mentioned “difficult” systems.

Ions in Water and Biophysical Implications
Ions in Water and Biophysical Implications

Author: Yizhak Marcus

Publisher: Springer Science & Business Media

Published: 2012-08-13

Total Pages: 224

ISBN-13: 9400746474

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Over the past decade, numerous books have attempted to explain ions in aqueous solutions in relation to biophysical phenomena. Ions in Water and Biophysical Implications, from Chaos to Cosmos offers a physicochemical point of view of the spread of this matter and suggests innovative solutions that will challenge the biophysics research establishment. Starting with a throughout discussion of the properties of liquid water, in particular as a structured liquid with an extensive hydrogen bonded structure, the book examines water as a solvent for gases, non-electrolytes, and electrolytes and reviews the properties, sizes and thermodynamics of isolated and aqueous ions, as well as their interactions, including those of polyelectrolytes. The effects of ions on water structure, including those on solvent dynamics and certain thermodynamic quantities, are presented. This volume investigates water surfaces with its vapour, with another liquid, and with a solid, as well as the effects of solutes, including simple ions and the water-miscible non-electrolytes. Surfaces are relevant to biomolecular and colloidal systems and the book discusses briefly surfactants, micelles and vesicles. Finally, the book concludes with a review of the various biophysical implications involving chaotropic and kosmotropic ions in homogeneous solutions and the Hofmeister series for ions concerning biomolecular and colloidal systems and some aspects of protein hydration and K+/Na+ selectivity in ion channels. Ions in Water and Biophysical Implications, from Chaos to Cosmos will appeal to physical chemists, biophysicists, biochemists, as well as to all students and researchers involved in the study of aqueous solutions.

Solvation Thermodynamics
Solvation Thermodynamics

Author: Arieh Y. Ben-Naim

Publisher: Springer Science & Business Media

Published: 2013-03-09

Total Pages: 253

ISBN-13: 1475765509

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This book deals with a subject that has been studied since the beginning of physical chemistry. Despite the thousands of articles and scores of books devoted to solvation thermodynamics, I feel that some fundamen tal and well-established concepts underlying the traditional approach to this subject are not satisfactory and need revision. The main reason for this need is that solvation thermodynamics has traditionally been treated in the context of classical (macroscopic) ther modynamics alone. However, solvation is inherently a molecular pro cess, dependent upon local rather than macroscopic properties of the system. Therefore, the starting point should be based on statistical mechanical methods. For many years it has been believed that certain thermodynamic quantities, such as the standard free energy (or enthalpy or entropy) of solution, may be used as measures of the corresponding functions of solvation of a given solute in a given solvent. I first challenged this notion in a paper published in 1978 based on analysis at the molecular level. During the past ten years, I have introduced several new quantities which, in my opinion, should replace the conventional measures of solvation thermodynamics. To avoid confusing the new quantities with those referred to conventionally in the literature as standard quantities of solvation, I called these "nonconventional," "generalized," and "local" standard quantities and attempted to point out the advantages of these new quantities over the conventional ones.

Transport Processes, Iono- and Osmoregulation
Transport Processes, Iono- and Osmoregulation

Author: R. Gilles

Publisher: Springer Science & Business Media

Published: 2012-12-06

Total Pages: 493

ISBN-13: 3642706134

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This volume is one of those published from the proceedings of the invited lectures to the First International Congress of Comparative Physiology and Biochemistry I organized at Liege (Belgium) in August 1984 under the auspices of the Section of Comparative Physiology and Biochemistry of the International Union of Biological Sciences. In a general foreword to these different volumes, it seems to me appropriate to consider briefly what may be the comparative approach. Living organisms, beyond the diversity of their morphological forms, have evolved a widespread range of basic solutions to cope with the different problems, both organismal and environmental with which they are faced. Soon after the turn of the century, some biologists realized that these solutions can be best comprehended in the frame work of a comparative approach integrating results of physiological and biochemical studies done at the organismic, cellular and molecular levels. The development of this approach amongst both physiologists and biochemists remained, however, extremely slow until recently.

Ionic Liquids II
Ionic Liquids II

Author: Barbara Kirchner

Publisher: Springer

Published: 2018-09-03

Total Pages: 295

ISBN-13: 3319897942

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​The series Topics in Current Chemistry Collections presents critical reviews from the journal Topics in Current Chemistry organized in topical volumes. The scope of coverage is all areas of chemical science including the interfaces with related disciplines such as biology, medicine and materials science. The goal of each thematic volume is to give the non-specialist reader, whether in academia or industry, a comprehensive insight into an area where new research is emerging which is of interest to a larger scientific audience. Each review within the volume critically surveys one aspect of that topic and places it within the context of the volume as a whole. The most significant developments of the last 5 to 10 years are presented using selected examples to illustrate the principles discussed. The coverage is not intended to be an exhaustive summary of the field or include large quantities of data, but should rather be conceptual, concentrating on the methodological thinking that will allow the non-specialist reader to understand the information presented. Contributions also offer an outlook on potential future developments in the field. The chapters “Ionic Liquid–Liquid Chromatography: A New General Purpose Separation Methodology”, “Proteins in Ionic Liquids: Current Status of Experiments and Simulations”, “Lewis Acidic Ionic Liquids” and "Quantum Chemical Modeling of Hydrogen Bonding in Ionic Liquids" are available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.