• Proceedings of the Korean Vacuum Society Conference
• /
• 2011.02a
• /
• pp.21-21
• /
• 2011

A series of Quasi-Elastic Neutron Scattering (QENS) experiments helps us to understand the single-particle (hydrogen atom) dynamics of a globular protein and its hydration water and strong coupling between them. We also performed Molecular Dynamics (MD) simulations on a realistic model of the hydrated hen-egg Lysozyme powder having two proteins in the periodic box. We found the existence of a Fragile-to-Strong dynamic Crossover (FSC) phenomenon in hydration water around a protein occurring at TL=$225{\pm}5K$ by analyzing Intermediate Scattering Function (ISF). On lowering of the temperature toward FSC, the structure of hydration water makes a transition from predominantly the High Density Liquid (HDL) form, a more fluid state, to predominantly the Low Density Liquid (LDL) form, a less fluid state, derived from the existence of a liquid?liquid critical point at an elevated pressure. We showed experimentally and confirmed theoretically that this sudden switch in the mobility of the hydration water around a protein triggers the dynamic transition (so-called glass transition) of the protein, at a temperature TD=220 K. Mean Square Displacement (MSD) is the important factor to show that the FSC is the key to the strong coupling between a protein and its hydration water by suggesting TL${\fallingdotseq}$TD. MD simulations with TIP4P force field for water were performed to understand hydration level dependency of the FSC temperature. We added water molecules to increase hydration level of the protein hydration water, from 0.30, 0.45, 0.60 and 1.00 (1.00 is the bulk water). These confirm the existence of the FSC and the hydration level dependence of the FSC temperature: FSC temperature is decreased upon increasing hydration level. We compared the hydration water around Lysozyme, B-DNA and RNA. Similarity among those suggests that the FSC and this coupling be universal for globular proteins, biopolymers.

• Food Science of Animal Resources
• /
• v.18 no.1
• /
• pp.35-41
• /
• 1998

The objective of this study was to examine the changes of physical properties by additions of different kinds of stabilizers milk proteins concentration, when stored at 4$^{\circ}C$ or 20$^{\circ}C$ for yoghurt. the results were summarized as follows: 1. Addition of 2% carboxyl methyl cellulose and carrageenan, gelation 0.4%, pectin and starch 0.6%, and carrageenan & pectin 0.8% in the manufacture of yoghurt increased the viscosity, water-holding capacity and protein hydration of yoghurt. 2. Addition of 3% skim milk powder, Ca-caseinate or Na-caseinate 0.6% increased the viscosity, water-holding capacity and protein hydration of yoghurt. 3. Twenty five percent of evaporation of milk promoted to build up the optimal structure of the micelles of yoghurt and improved viscosity, water-holding capacity and protein hydration of yoghurt. 4. Addition of stabilizers to yoghurt showed an increase of viscosity, water-holding capacity and protein hydration when compared with non-addition of stabilizers to yoghurt at 4$^{\circ}C$, 20$^{\circ}C$ storage for 12hrs, 96hrs followed by the decrease of it.

• Proceeding of EDISON Challenge
• /
• 2014.03a
• /
• pp.103-113
• /
• 2014

Hydrophobicity is the key concept to understand the role of water in protein folding, protein self-assembly, and protein-ligand interaction. Conventionally, hydrophobicity of amino acids in a protein has been argued based on hydrophobicity scales determined for individual free amino acids, assuming that those scales are unaltered when amino acids are embedded in a protein. Here, we investigate how the hydrophobicity of constituent amino acids depends on the protein context, in particular, on the total charge and secondary structures of a protein. To this end, we compute and analyze the hydration free energy - free energy change upon hydration quantifying the hydrophobicity - of three short proteins based on the integral-equation theory of liquids. We find that the hydration free energy of charged amino acids is significantly affected by the protein total charge and exhibits contrasting behavior depending on the protein net charge being positive or negative. We also observe that amino acids in the central ${\beta}$-strand sandwiched by ${\beta}$-sheets display more enhanced hydrophobicity than free amino acids, whereas those in the ${\alpha}$-helix do not clearly show such a tendency. Our results provide novel insights into the hydrophobicity of amino acids, and will be valuable for rationalizing and predicting the strength of water-mediated interaction involved in the biological activity of proteins.

• Proceeding of EDISON Challenge
• /
• 2016.03a
• /
• pp.163-166
• /
• 2016

Hydrophobicity is the key concept to understand the water plays in protein folding, protein aggregation, and protein-protein interaction. Traditionally, the hydrophobicity of protein is defined based on the scales of the hydrophobicity of residue, assuming that the hydrophobicity of free amino acids is maintained. Here, we explore how the hydrophobicity of constituting amino acids in protein rely on the protein context, in particular, on the total charge and secondary structures of a protein. To this end, we calculate and investigate the hydration free energy of three short proteins based on the integral-equation theory of liquids. We find that the hydration free energy of charged amino acids is significantly affected by the protein total charge and exhibits contrasting behavior depending on the protein total charge being positive or negative. We also observe that amino acids in the ${\beta}-sheets$ display more enhanced the hydrophobicity than amino acids in the loop, whereas those in the ${\alpha}-helix$ do not clearly show such a tendency. And the salt-bridge forming amino acids also exhibit increase of the hydrophobicity than that with no salt bridge. Our results provide novel insights into the hydrophobicity of amino acids, and will be valuable for rationalizing and predicting the strength of water-mediated interaction involved in the biological activity of proteins.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.35 no.6
• /
• pp.627-632
• /
• 2002

This study was investigated the changes of gel properties about pH, color and water holding capacity at various hydration time and temperature of food-grade additives (BPP: bovine plasma protein, DEW: dried egg white, SPI: soy protein isolate). The changes of rheological properties were checked about hydration time and temperature. Hydration time and temperature affected pH value, hydration decreased pH of SPI and DEW. The BPP was not influenced at hydration time and temperature. Some Hydration condition increased jelly strength of food-grade additive, but SPI did not form a gel at all hydration condition. Hydration increased lightness of food-protein.

• Journal of the Society of Cosmetic Scientists of Korea
• /
• v.42 no.4
• /
• pp.343-349
• /
• 2016

Many minerals and nutrient salts are abundant in Jeju lava sea water. The objective of this study was to evaluate the skin hydration effects of Jeju lava sea water. The skin barrier serves as a protective barrier that prevents the loss of moisture. The water holding capacity and water transport of the epidermis have been proposed to be important determinants of skin hydration. Jeju lava sea water increased the mRNA expression of filaggrin and caspase-14 which is related to natural moisturizing factor (NMF) formation. Aquaporins 3 (AQP3) are proteins that facilitate the transport of water across cell membranes. Jeju lava sea water increased the mRNA expression and protein expression of AQP3. We employed a skin equivalent model to assess the efficacy of Jeju lava sea water. In a skin equivalent model, Jeju lava sea water increased the CD44 (hyaluronic acid receptor) which is related to skin hydration. From these results, we found out Jeju lava sea water maybe help to skin hydration.

• Applied Biological Chemistry
• /
• v.28 no.2
• /
• pp.62-67
• /
• 1985

Hydration rate of 35 Japonica and 24 J x Indica rice varieties at $23^{\circ}C$ was investigated and an attempt was made for a tentative classification of milled rice into six groups based on hydration rate. Each rice variety had characteristic value for hydration rate. In general, J x Indica rice hydrated at a faster rate than Japonica rice. Hydration rate was negatively correlated with the ratio of length to width of rice grain. No correlation was found between hydration rate and protein, amylose, surface area, volume or initial water grain.

• Preventive Nutrition and Food Science
• /
• v.20 no.1
• /
• pp.15-21
• /
• 2015

The skin plays a key role in protecting the body from the environment and from water loss. Cornified envelope (CE) and natural moisturizing factor (NMF) are considered as the primary regulators of skin hydration and barrier function. The CE prevents loss of water from the body and is formed by cross-linking of several proteins. Among these proteins, filaggrin is an important protein because NMF is produced by the degradation of filaggrin. Proteases, including matriptase and prostasin, stimulate the generation of filaggrin from profilaggrin and caspase-14 plays a role in the degradation of filaggrin. This study elucidated the effects of an ethanol extract of Boesenbergia pandurata (Roxb.) Schltr., known as fingerroot, and its active compound panduratin A on CE formation and filaggrin processing in HaCaT, human epidermal keratinocytes. B. pandurata extract (BPE) and panduratin A significantly stimulated not only CE formation but also the expression of CE proteins, such as loricrin, involucrin, and transglutaminase, which were associated with $PPAR{\alpha}$ expression. The mRNA and protein levels of filaggrin and filaggrin-related enzymes, such as matriptase, prostasin, and caspase-14 were also up-regulated by BPE and panduratin A treatment. These results suggest that BPE and panduratin A are potential nutraceuticals which can enhance skin hydration and barrier function based on their CE formation and filaggrin processing.

• Proceedings of the Korean Society of Near Infrared Spectroscopy Conference
• /
• 2001.06a
• /
• pp.1286-1286
• /
• 2001

Despite extensive theoretical and experimental studies the structure of the protein-solvent interface is subject of many controversy. Understanding the processes that occur in aqueous solution requires understanding of the solvent influence on the structure of protein. The aim of this study is to investigate the applicability of NIR methods in the study of hydration phenomena in protein solutions. Temperature-induced changes in NIR spectra of -lactoglobulin (BLG) in aqueous solutions have been investigated by means of two-dimensional correlation spectroscopy (2DCOS) and principal component analysis (PCA). With the temperature increase the balance of forces between the BLG's interaction with itself and the BLGs interaction with its environment is disrupted leading to BLG unfolding. Significant differences of 2D signals and distinct discrepancies of loading on PC1 and PC2 were observed as a result of temperature increase. In the native folded conformation of BLC, most of the nonpolar amino acids are hidden in the centre of the structure, out of contact with water molecules, while charged groups are outside, in the contact with water. The polar groups promote low density Ih-type structure in the water outside this first hydration shell. When BLG unfolds it assumes a more extended configuration on which the previously buried nonpolar groups are exposed to water and promote the higher density II-type structure outside its first shell. Detailed assignments of bands attributed to the bulk water, different states of the hydrated water and the changed conformation of BLG are proposed.

• Bulletin of the Korean Chemical Society
• /
• v.2 no.2
• /
• pp.66-71
• /
• 1981

The effects of cation on tRNA have been theoretically investigated using the semiempirical potential energy functions. The binding of $Mg^{2+}$ to the model compound and the hydration scheme of the anticodon loop have been determined, and their stabilization energies produced by the introduction of magnesium pentahydrate and water molecules in the first hydration shell were calculated. The results indicate that magnesium pentahydrate is important for decreasing the flexibility of the anticodon loop and satisfying the large Y37 stereochemically during the protein synthesis. The effects of $Mg^{2+}$ on the hydration scheme were also investigated.