Water adsorption on carbon - A review

High-yield solar-driven atmospheric water harvesting of metal–organic-framework-derived nanoporous carbon with fast-diffusion water channels

Motivation Understanding the molecular mechanisms of thermal stability is a challenge in protein biology. Indeed, knowing the temperature at which proteins are stable has important theoretical implications, which are intimately linked with properties of the native fold, and a wide range of potential applications from drug design to the optimization of enzyme activity. Results Here, we present a novel graph-theoretical framework to assess thermal stability based on the structure without any a priori information. In this approach we describe proteins as energy-weighted graphs and compare them using ensembles of interaction networks. Investigating the position of specific interactions within the 3D native structure, we developed a parameter-free network descriptor that permits to distinguish thermostable and mesostable proteins with an accuracy of 76% and area under the receiver operating characteristic curve of 78%. Availability and implementation Code is available upon request to edoardo.milanetti@uniroma1.it. Supplementary information Supplementary data are available at Bioinformatics online.

Insights on protein thermal stability: a graph representation of molecular interactions

Mandarin fish that have been prepared and chilled have a shelf life of 4 days at 4°C storage, according to the total volatile basic nitrogen values. During the storage process, we observed that the texture characteristics of these fish significantly deteriorated. Certain low-abundance proteins were degraded during the shelf life, which resulted in changes in protein conformation and protein–water interaction patterns. The water-holding capacity of the fish decreased during 4°C storage; nuclear magnetic resonance analysis showed that the binding of water in fish was weakened as shelf storage prolonged and a portion of the free water was also “squeezed” to the surface of the fish in the later stages of storage. A correlation analysis showed that a decrease in the immobilized water content and mobility was associated with quality deterioration of the fish, which may be a result of increase in hydrophobic interaction and disulfide bonds in the fish during storage.

https://www.tandfonline.com/doi/pdf/10.1080/10942912.2018.1451343

Texture characteristics of chilled prepared Mandarin fish (Siniperca chuatsi) during storage

Temperature dependence of water adsorption on highly graphitized carbon black and highly ordered mesoporous carbon

Properties of liquids at solid interfaces play a central role in numerous important processes in nature. Nuclear magnetic resonance (NMR) is particularly useful for probing liquid/graphitic carbon interfacial properties. In particular, the nucleus-independent chemical shift (NICS) provides a sensitive measure of the distance between adsorbates and the graphitic carbon surface on the subnanometer scale, enabling NMR to acquire subnanometer scale spatial resolution. Here, by combining the information on thermodynamics obtained from in situ NMR-detected water isotherm and spatially resolved information on structure and dynamics obtained by NICS-resolved NMR, the microscopic process of water nucleation and growth inside the micropore of activated carbons is investigated. The formation of water clusters at surface sites, the cooperative growth process of pore bridging, and the final stage of horizontal pore filling are revealed in detail, demonstrating the potential of this comprehensive NMR approach for study...

Nucleation and Growth Process of Water Adsorption in Micropores of Activated Carbon Revealed by NMR

Water plays an important role in weak associations of small drug molecules with proteins. Intense focus has been on binding-induced structural changes in the water network surrounding protein binding sites, especially their contributions to binding thermodynamics. However, water is also tightly coupled to protein conformations and dynamics, and so far little is known about the influence of water-protein interactions on ligand binding. Alcohols are a type of low-affinity drugs, and it remains unclear how water affects alcohol-protein interactions. Here, we present alcohol adsorption isotherms under controlled protein hydration using in situ NMR detection. As functions of hydration level, Gibbs free energy, enthalpy, and entropy of binding were determined from the temperature dependence of isotherms. Two types of alcohol binding were found. The dominant type is low-affinity nonspecific binding, which is strongly dependent on temperature and the level of hydration. At low hydration levels, this nonspecific binding only occurs above a threshold of alcohol vapor pressure. An increased hydration level reduces this threshold, with it finally disappearing at a hydration level of h ≈ 0.2 (g water/g protein), gradually shifting alcohol binding from an entropy-driven to an enthalpy-driven process. Water at charged and polar groups on the protein surface was found to be particularly important in enabling this binding. Although further increase in hydration has smaller effects on the changes of binding enthalpy and entropy, it results in a significant negative change in Gibbs free energy due to unmatched enthalpy-entropy compensation. These results show the crucial role of water-protein interplay in alcohol binding.

/pdf/dominant-alcohol-protein-interaction-via-hydration-enabled-1by16iw0g8.pdf

Dominant Alcohol-Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism.

Protein dynamics and thermodynamics crossover at 10 °C: Different roles of hydration at hydrophilic and hydrophobic groups

Water plays an important role in weak associations of small drug molecules with proteins. Intense focus has been on binding-induced structural changes in the water network surrounding protein binding sites, especially their contributions to binding thermodynamics. However, water is also tightly coupled to protein conformations and dynamics, and so far little is known about the influence of water–protein interactions on ligand binding. Alcohols are a type of low-affinity drugs, and it remains unclear how water affects alcohol–protein interactions. Here, we present alcohol adsorption isotherms under controlled protein hydration using in situ NMR detection. As functions of hydration level, Gibbs free energy, enthalpy, and entropy of binding were determined from the temperature dependence of isotherms. Two types of alcohol binding were found. The dominant type is low-affinity nonspecific binding, which is strongly dependent on temperature and the level of hydration. At low hydration levels, this nonspecific binding only occurs above a threshold of alcohol vapor pressure. An increased hydration level reduces this threshold, with it finally disappearing at a hydration level of h ≈ 0.2 (g water/g protein), gradually shifting alcohol binding from an entropy-driven to an enthalpy-driven process. Water at charged and polar groups on the protein surface was found to be particularly important in enabling this binding. Although further increase in hydration has smaller effects on the changes of binding enthalpy and entropy, it results in a significant negative change in Gibbs free energy due to unmatched enthalpy–entropy compensation. These results show the crucial role of water–protein interplay in alcohol binding.

Dominant Alcohol–Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism

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Papers

Nucleation and Growth Process of Water Adsorption in Micropores of Activated Carbon Revealed by NMR

Dominant Alcohol-Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism.

Protein dynamics and thermodynamics crossover at 10 °C: Different roles of hydration at hydrophilic and hydrophobic groups

Dominant Alcohol–Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism