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Journal ArticleDOI

Why forces between proteins follow different Hofmeister series for pH above and below pI.

TLDR
Numerical results that include non-electrostatic ion-specific forces acting that are ignored in classical electrolyte and double layer theory are given here for model calculations of the force between two model charge-regulated hen-egg-white protein surfaces.
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This article is published in Biophysical Chemistry.The article was published on 2005-10-03. It has received 197 citations till now. The article focuses on the topics: Hofmeister series.

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Citations
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Transport phenomena in nanofluidics

TL;DR: In this paper, the authors investigated the transport properties of 50-nm-high 1D nanochannels on a chip and showed that they can be used for the separation and preconcentration of proteins.
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Chemistry of Hofmeister anions and osmolytes.

TL;DR: A mechanism for specific ion effects is elucidated for aqueous systems containing charged and uncharged polymers, polypeptides, and proteins and a hydrogen-bonding mechanism is tested for the urea denaturation of proteins with some of these same systems.
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Polymeric materials based on silk proteins

TL;DR: In this article, the structure and function of silk proteins produced naturally by silkworms and spiders are discussed, followed by the biological and technical processing of Silk proteins into a variety of morphologies (including capsules, fibers, films, foams, gels and spheres).
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Protein–excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development

TL;DR: Key mechanisms of protein-excipient interactions such as electrostatic and cation-pi interactions, preferential hydration, dispersive forces, and hydrogen bonding are presented in the context of different physical states of the formulation.
References
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Journal ArticleDOI

The Hofmeister effect and the behaviour of water at interfaces.

TL;DR: The first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air-water interface is proposed; this mechanism suggests a simple model for the behaviour of water at all interfaces, regardless of whether the non-aqueous component is neutral or charged, polar or non-polar.
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‘Zur Lehre von der Wirkung der Salze’ (about the science of the effect of salts): Franz Hofmeister's historical papers

TL;DR: In a seminal series of papers, Franz Hofmeister, Professor of Pharmacology at the University of Prague, was the first to study specific ion effects systematically as discussed by the authors, which stands in the scheme of things in importance much as did the work of Mendel to genetics.
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Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process.

TL;DR: The surface potential difference and surface tension at an air-salt solution interface are used to generate a simple model for how ions affect protein stability and solubility through indirect interactions at the protein-solution interface.
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The present state of affairs with Hofmeister effects

TL;DR: The present state of affairs, theory and experiment with Hofmeister effects is reviewed in this article, where the authors present a review of the literature and experiment results of their work.
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Molecular Structure of Salt Solutions: A New View of the Interface with Implications for Heterogeneous Atmospheric Chemistry

TL;DR: In this article, the authors report results from molecular dynamics simulations of a series of sodium halide solution/air interfaces and develop a molecular picture of hydrogen bonding in the interfacial region that might be tested by surface sensitive spectroscopic experiments.
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