Journal ArticleDOI
A View of the Hydrophobic Effect
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TLDR
Experimental and theoretical studies of nonpolar solute partitioning into water are surveyed and it is noted that the hydrophobic effect is not just due to “water ordering” and not merely due to small size effects of water.Abstract:
Oil and water do not mix. The disaffinity of oil for water, with its unusual temperature dependence, is called the hydrophobic effect. It is important to understand the factors underlying the hydrophobic effect because they appear to play key roles in membrane and micelle formation, protein folding, ligand-protein and protein−protein binding, chromatographic retention, possibly nucleic acid interactions, and the partitioning of drugs, metabolites, and toxins throughout the environment and living systems. Here, we survey experimental and theoretical studies of nonpolar solute partitioning into water. We note that the hydrophobic effect is not just due to “water ordering” and not merely due to small size effects of water. The properties vary substantially with temperature and solute shape. Also, we discuss the limitations of using oil/water partitioning as the basis for some thermodynamic models in chemistry and biology.read more
Citations
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Noncovalent Functionalization of Graphene and Graphene Oxide for Energy Materials, Biosensing, Catalytic, and Biomedical Applications
Vasilios Georgakilas,Jitendra N. Tiwari,K. Christian Kemp,Jason A. Perman,Athanasios B. Bourlinos,Kwang S. Kim,Radek Zboril +6 more
TL;DR: This Review focuses on noncovalent functionalization of graphene and graphene oxide with various species involving biomolecules, polymers, drugs, metals and metal oxide-based nanoparticles, quantum dots, magnetic nanostructures, other carbon allotropes, and graphene analogues.
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Water as an Active Constituent in Cell Biology
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Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
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A Medicinal Chemist’s Guide to Molecular Interactions
TL;DR: This article compile and review the literature on molecular interactions as it pertains to medicinal chemistry through a combination of careful statistical analysis of the large body of publicly available X-ray structure data and experimental and theoretical studies of specific model systems.
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Thermoresponsive hydrogels in biomedical applications.
Leda Klouda,Antonios G. Mikos +1 more
TL;DR: The scope of this paper is to review the aqueous polymer solutions that exhibit transition to gel upon temperature change and focuses mainly on hydrogels based on natural polymers as well as poly(ethylene glycol)-biodegradable polyester copolymers.
References
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Book ChapterDOI
Some factors in the interpretation of protein denaturation.
TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Journal ArticleDOI
Dominant forces in protein folding
TL;DR: The present review aims to provide a reassessment of the factors important for folding in light of current knowledge, including contributions to the free energy of folding arising from electrostatics, hydrogen-bonding and van der Waals interactions, intrinsic propensities, and hydrophobic interactions.
Journal ArticleDOI
Semianalytical treatment of solvation for molecular mechanics and dynamics
TL;DR: In this paper, it was shown that the active carbon incorporation catalyst is carbided iron and this conclusion was well supported by bulk carbon to iron stoichiometries of 0.1-0.25 estimated from the TPHT peak areas which were adequate to represent 40-60'36 conversion to bulk carbides such as Fe,C or FeSC2.
Book
The Hydrophobic Effect: Formation of Micelles and Biological Membranes
TL;DR: In this article, the authors discuss the properties of water molecules and their relationship with common soluble proteins, such as membrane proteins and membrane membrane proteins, as well as the effect of temperature on their properties.
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