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- Boström, Mathias, et al.
(författare)
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Modifying the Poisson-Boltzmann Approach to Model Specific Ion Effects
- 2010
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Ingår i: Specific Ion Effects. - Singapore : World Scientific Publishing Co. Pte. Ltd.. - 9789814271578 ; , s. 293-309
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Specific ion effects are important in numerous fields of science and technology. They have been discussed for over 100 years, ever since the pioneering work done by Franz Hofmeister and his group in Prague. Over the last decades, hundreds of examples have been published and periodically explanations have been proposed. However, it is only recently that a profound understanding of the basic effects and their reasons could be achieved. Today, we are not far from a general explanation of specific ion effects. This book summarizes the main new ideas that have come up in the last ten years.In this book, the efforts of theoreticians are substantially supported by the experimental results stemming from new and exciting techniques. Both the new theoretical concepts and the experimental landmarks are collected and critically discussed by eminent scientists and well-known specialists in this field. Beyond the rigorous explanations, guidelines are given to non-specialists in order to help them understand the general rules governing specific ion effects in chemistry, biology, physics and engineering.
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| 2. |
- Lund, Mikael, et al.
(författare)
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Ion binding to biomolecules
- 2009
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Ingår i: Specific Ion Effects. - : WORLD SCIENTIFIC. - 9789814271585 - 9789814468176 - 9789814271578 ; , s. 217-230
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Bokkapitel (refereegranskat)abstract
- We investigated specific anion binding to basic amino acid residues as well as to a range of patchy protein models. This microscopic information was subsequently used to probe protein–protein interactions for aqueous lysozyme solutions. Using computer simulations to study both atomistic and coarse grained protein molecules, it is shown that the ion–protein interaction mechanism as well as magnitude is largely controlled by the nature of the interfacial amino acid residues. Small anions interact with charged side-chains via ionpairing while larger, poorly hydrated anions are attracted to nonpolar residues due to a number of solvent-assisted mechanisms. Taking into account ion and surface specificity in a mesoscopic model for protein–protein interactions, we investigated the association of the protein lysozyme in aqueous solutions of sodium iodide and sodium chloride. As observed experimentally, it is found that ‘salting out’ of lysozyme follows the reverse Hofmeister series for pH below the iso-electric point and the direct series for pH above.
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