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Artykuły w czasopismach na temat „Protein-water systems”

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Data publikacji: 6 września 2023

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1

Barkalov, I. M., A. I. Bolshakov, V. I. Goldanskii i Yu F. Krupyanskii. "Vitrification effects in water—protein systems". Chemical Physics Letters 208, nr 1-2 (czerwiec 1993): 1–4. http://dx.doi.org/10.1016/0009-2614(93)80066-x.

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Versace, Rodney E., i Themis Lazaridis. "Modeling Protein–Micelle Systems in Implicit Water". Journal of Physical Chemistry B 119, nr 25 (15.06.2015): 8037–47. http://dx.doi.org/10.1021/acs.jpcb.5b00171.

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3

Versace, Rodney E., i Themis Lazaridis. "Modelling Protein-Micelle Systems in Implicit Water". Biophysical Journal 108, nr 2 (styczeń 2015): 249a. http://dx.doi.org/10.1016/j.bpj.2014.11.1378.

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4

Palacios, Aida C., Carlo Sarnthein-Graf i Camillo La Mesa. "Equilibrium between phases in water–protein–surfactant systems". Colloids and Surfaces A: Physicochemical and Engineering Aspects 228, nr 1-3 (listopad 2003): 25–35. http://dx.doi.org/10.1016/s0927-7757(03)00332-7.

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5

Vorob’ev, Mikhail. "Monitoring of water ordering in aqueous protein systems". Food Hydrocolloids 21, nr 2 (marzec 2007): 309–12. http://dx.doi.org/10.1016/j.foodhyd.2006.06.001.

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6

Goncharuk, Elena, Galyna Polishchuk, Iryna Shevchenko i Tetiana Osmak. "Nature of water bonding in hydrated milk-protein systems". Ukrainian Food Journal 9, nr 1 (marzec 2020): 111–19. http://dx.doi.org/10.24263/2304-974x-2020-9-1-10.

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7

Tombs, M. P., B. G. Newsom i P. Wilding. "PROTEIN SOLUBILITY: PHASE SEPARATION IN ARACHIN-SALT-WATER SYSTEMS". International Journal of Peptide and Protein Research 6, nr 4 (12.01.2009): 253–77. http://dx.doi.org/10.1111/j.1399-3011.1974.tb02384.x.

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8

Potes, Naritchaya, Joseph P. Kerry i Yrjö H. Roos. "Protein Modifications in High Protein-Oil and Protein-Oil-Sugar Systems at Low Water Activity". Food Biophysics 9, nr 1 (25.08.2013): 49–60. http://dx.doi.org/10.1007/s11483-013-9316-1.

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9

Bellavia, Giuseppe, Sergio Giuffrida, Grazia Cottone, Antonio Cupane i Lorenzo Cordone. "Protein Thermal Denaturation and Matrix Glass Transition in Different Protein−Trehalose−Water Systems". Journal of Physical Chemistry B 115, nr 19 (19.05.2011): 6340–46. http://dx.doi.org/10.1021/jp201378y.

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10

Martini, Silvia, Claudia Bonechi, Alberto Foletti i Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics". Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.

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Water-protein interactions help to maintain flexible conformation conditions which are required for multifunctional protein recognition processes. The intimate relationship between the protein surface and hydration water can be analyzed by studying experimental water properties measured in protein systems in solution. In particular, proteins in solution modify the structure and the dynamics of the bulk water at the solute-solvent interface. The ordering effects of proteins on hydration water are extended for several angstroms. In this paper we propose a method for analyzing the dynamical properties of the water molecules present in the hydration shells of proteins. The approach is based on the analysis of the effects of protein-solvent interactions on water protons NMR relaxation parameters. NMR relaxation parameters, especially the nonselective (R1NS) and selective (R1SE) spin-lattice relaxation rates of water protons, are useful for investigating the solvent dynamics at the macromolecule-solvent interfaces as well as the perturbation effects caused by the water-macromolecule interactions on the solvent dynamical properties. In this paper we demonstrate that Nuclear Magnetic Resonance Spectroscopy can be used to determine the dynamical contributions of proteins to the water molecules belonging to their hydration shells.

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11

Ghosh, Rikhia, Saikat Banerjee, Milan Hazra, Susmita Roy i Biman Bagchi. "Sensitivity of polarization fluctuations to the nature of protein-water interactions: Study of biological water in four different protein-water systems". Journal of Chemical Physics 141, nr 22 (14.12.2014): 22D531. http://dx.doi.org/10.1063/1.4902821.

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12

Kimmich, R., T. Gneiting, K. Kotitschke i G. Schnur. "Fluctuations, exchange processes, and water diffusion in aqueous protein systems". Biophysical Journal 58, nr 5 (listopad 1990): 1183–97. http://dx.doi.org/10.1016/s0006-3495(90)82459-0.

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13

Luchinat, Claudio, Giacomo Parigi i Enrico Ravera. "Water and Protein Dynamics in Sedimented Systems: A Relaxometric Investigation". ChemPhysChem 14, nr 13 (13.05.2013): 3156–61. http://dx.doi.org/10.1002/cphc.201300167.

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14

Morén, Anna Karin, i Ali Khan. "Phase Behavior and Phase Structure of Protein–Surfactant–Water Systems". Journal of Colloid and Interface Science 218, nr 2 (październik 1999): 397–403. http://dx.doi.org/10.1006/jcis.1999.6433.

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15

Zaccai, G. "The effect of water on protein dynamics". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, nr 1448 (29.08.2004): 1269–75. http://dx.doi.org/10.1098/rstb.2004.1503.

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Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.

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16

López-Díez, E. Consuelo, i Stephen Bone. "An investigation of the water-binding properties of protein + sugar systems". Physics in Medicine and Biology 45, nr 12 (7.11.2000): 3577–88. http://dx.doi.org/10.1088/0031-9155/45/12/305.

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17

Hayashi, Yoshihito, Ikuya Oshige, Yoichi Katsumoto, Shinji Omori i Akio Yasuda. "Protein–solvent interaction in urea–water systems studied by dielectric spectroscopy". Journal of Non-Crystalline Solids 353, nr 47-51 (grudzień 2007): 4492–96. http://dx.doi.org/10.1016/j.jnoncrysol.2007.02.079.

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18

Maidannyk, V. A., i Y. H. Roos. "Water sorption, glass transition and “strength” of lactose – Whey protein systems". Food Hydrocolloids 70 (wrzesień 2017): 76–87. http://dx.doi.org/10.1016/j.foodhyd.2017.03.025.

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19

Kato, Masaru, Jenny Z. Zhang, Nicholas Paul i Erwin Reisner. "Protein film photoelectrochemistry of the water oxidation enzyme photosystem II". Chem. Soc. Rev. 43, nr 18 (2014): 6485–97. http://dx.doi.org/10.1039/c4cs00031e.

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20

Kodali, Goutham, Joshua A. Mancini, Lee A. Solomon, Tatiana V. Episova, Nicholas Roach, Christopher J. Hobbs, Pawel Wagner i in. "Design and engineering of water-soluble light-harvesting protein maquettes". Chemical Science 8, nr 1 (2017): 316–24. http://dx.doi.org/10.1039/c6sc02417c.

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Design of nanometer scale artificial light harvesting and charge separating proteins enables reengineering to overcome the limitations of natural selection for efficient systems that better meet human energetic needs.

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21

Wouters, Arno GB, i Jan A. Delcour. "Cereal protein-based nanoparticles as agents stabilizing air–water and oil–water interfaces in food systems". Current Opinion in Food Science 25 (luty 2019): 19–27. http://dx.doi.org/10.1016/j.cofs.2019.02.002.

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22

Cornacchia, Leonardo, i Yrjö H. Roos. "Stability of β-Carotene in Protein-Stabilized Oil-in-Water Delivery Systems". Journal of Agricultural and Food Chemistry 59, nr 13 (13.07.2011): 7013–20. http://dx.doi.org/10.1021/jf200841k.

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23

Guan, Tongwei, Zhiheng Zhang, Xiaojing Li, Shaoning Cui, David Julian McClements, Xiaotian Wu, Long Chen i in. "Preparation, Characteristics, and Advantages of Plant Protein-Based Bioactive Molecule Delivery Systems". Foods 11, nr 11 (26.05.2022): 1562. http://dx.doi.org/10.3390/foods11111562.

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As a renewable resource, the market trend of plant protein has increased significantly in recent years. Compared with animal protein, plant protein production has strong sustainability factors and a lower environmental impact. Many bioactive substances have poor stability, and poor absorption effects limit their application in food. Plant protein-based carriers could improve the water solubility, stability, and bioavailability of bioactive substances by different types of delivery systems. In this review, we present a detailed and concise summary of the effects and advantages of various plant protein-based carriers in the encapsulation, protection, and delivery of bioactive substances. Furthermore, the research progress of food-grade bioactive ingredient delivery systems based on plant protein preparation in recent years is summarized, and some current challenges and future research priorities are highlighted. There are some key findings and conclusions: (i) plant proteins have numerous functions: as carriers for transportation systems, a shell or core of a system, or food ingredients; (ii) plant protein-based carriers could improve the water solubility, stability, and bioavailability of bioactive substances by different types of delivery systems; and (iii) plant protein-based carriers stabilize bioactive substances with potential applications in the food and nutrition fields.

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24

Morón, M. C. "Protein hydration shell formation: Dynamics of water in biological systems exhibiting nanoscopic cavities". Journal of Molecular Liquids 337 (wrzesień 2021): 116584. http://dx.doi.org/10.1016/j.molliq.2021.116584.

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25

Heyn, Timon R., Maximilian J. Uttinger, Arno Kwade, Wolfgang Peukert, Julia K. Keppler i Karin Schwarz. "Whey protein (amyloid)-aggregates in oil-water systems: The process-related comminution effect". Journal of Food Engineering 311 (grudzień 2021): 110730. http://dx.doi.org/10.1016/j.jfoodeng.2021.110730.

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26

Yoshioki, Shuzo. "Formulation of the Hessian Matrix for the Conformational Energy of Protein-Water Systems". Journal of the Physical Society of Japan 66, nr 9 (15.09.1997): 2927–35. http://dx.doi.org/10.1143/jpsj.66.2927.

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27

Rorschach, H. E., i C. F. Hazlewood. "Protein dynamics and the NMR relaxation time T1 of water in biological systems". Journal of Magnetic Resonance (1969) 70, nr 1 (październik 1986): 79–88. http://dx.doi.org/10.1016/0022-2364(86)90364-1.

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28

Krupyanskii, Yu F., V. I. Goldanskii, G. U. Nienhaus i F. Parak. "Dynamics of protein-water systems revealed by Rayleigh scattering of Mössbauer radiation (RSMR)". Hyperfine Interactions 53, nr 1-4 (lipiec 1990): 59–73. http://dx.doi.org/10.1007/bf02101039.

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29

Kruk, Danuta, Adam Kasparek, Elzbieta Masiewicz, Karol Kolodziejski, Radoslaw Cybulski i Bartosz Nowak. "Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry". International Journal of Molecular Sciences 24, nr 4 (17.02.2023): 4093. http://dx.doi.org/10.3390/ijms24044093.

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1H spin-lattice relaxation experiments have been performed for water–Bovine Serum Albumin (BSA) mixtures, including 20%wt and 40%wt of BSA. The experiments have been carried out in a frequency range encompassing three orders of magnitude, from 10 kHz to 10 MHz, versus temperature. The relaxation data have been thoroughly analyzed in terms of several relaxation models with the purpose of revealing the mechanisms of water motion. For this purpose, four relaxation models have been used: the data have been decomposed into relaxation contributions expressed in terms of Lorentzian spectral densities, then three-dimensional translation diffusion has been assumed, next two-dimensional surface diffusion has been considered, and eventually, a model of surface diffusion mediated by acts of adsorption to the surface has been employed. In this way, it has been demonstrated that the last concept is the most plausible. Parameters describing the dynamics in a quantitative manner have been determined and discussed.

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30

Giussani, Lara, Gloria Tabacchi, Salvatore Coluccia i Ettore Fois. "Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels". International Journal of Molecular Sciences 20, nr 12 (18.06.2019): 2965. http://dx.doi.org/10.3390/ijms20122965.

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Incorporation of biological systems in water nanodroplets has recently emerged as a new frontier to investigate structural changes of biomolecules, with perspective applications in ultra-fast drug delivery. We report on the molecular dynamics of the digestive protein Pepsin subjected to a double confinement. The double confinement stemmed from embedding the protein inside a water nanodroplet, which in turn was caged in a nanochannel mimicking the mesoporous silica SBA-15. The nano-bio-droplet, whose size fits with the pore diameter, behaved differently depending on the protonation state of the pore surface silanols. Neutral channel sections allowed for the droplet to flow, while deprotonated sections acted as anchoring piers for the droplet. Inside the droplet, the protein, not directly bonded to the surface, showed a behavior similar to that reported for bulk water solutions, indicating that double confinement should not alter its catalytic activity. Our results suggest that nanobiodroplets, recently fabricated in volatile environments, can be encapsulated and stored in mesoporous silicas.

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31

Hambly, A. C., R. K. Henderson, A. Baker, R. M. Stuetz i S. J. Khan. "Fluorescence monitoring for cross-connection detection in water reuse systems: Australian case studies". Water Science and Technology 61, nr 1 (1.01.2010): 155–62. http://dx.doi.org/10.2166/wst.2010.795.

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A rapid, highly sensitive method for detection of cross-connections between recycled and potable water in dual reticulation systems is required. The aim of this research was to determine the potential of fluorescence spectroscopy as a monitoring tool at three Australian dual distribution (drinking and recycled water) systems. Weekly grab samples of recycled and potable water were obtained over 12 weeks at each site and analysed for fluorescence excitation-emission matrix (EEM) spectroscopy, UV254, dissolved organic carbon (DOC), electrical conductivity and pH. Fluorescence EEM spectroscopy was able to differentiate between recycled and potable water at each site by monitoring the protein-like fluorescence at peak T—an excitation-emission wavelength pair of λex/em = 300/350 nm. While electrical conductivity was also able to distinguish between recycled and potable water, the differentiation was greatest when using fluorescence. For example, the peak T fluorescence in recycled water was up to 10 times that of potable water in comparison with electrical conductivity that had a maximum 5 times differentiation. Furthermore, by comparing the protein-like fluorescence at peak T and humic-like fluorescence at peak A (λex/em = 235/426 nm), the three different recycled water systems were able to be differentiated. Overall, fluorescence shows promise as a monitoring tool for detecting cross-connections.

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32

Özeren, Hüsamettin D., Xin-Feng Wei, Fritjof Nilsson, Richard T. Olsson i Mikael S. Hedenqvist. "Role of hydrogen bonding in wheat gluten protein systems plasticized with glycerol and water". Polymer 232 (październik 2021): 124149. http://dx.doi.org/10.1016/j.polymer.2021.124149.

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33

Costantino, H. "Water sorption behavior of lyophilized protein–sugar systems and implications for solid-state interactions". International Journal of Pharmaceutics 166, nr 2 (18.05.1998): 211–21. http://dx.doi.org/10.1016/s0378-5173(98)00050-7.

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Szuminska, Katarzyna, Aleksander Gutsze i Andrzej Kowalczyk. "Relaxation of Water Protons in Highly Concentrated Aqueous Protein Systems Studied by NMR Spectroscopy". Zeitschrift für Naturforschung C 56, nr 11-12 (1.12.2001): 1075–81. http://dx.doi.org/10.1515/znc-2001-11-1226.

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Abstract In this paper we present proton spin-lattice ( T1) and spin-spin ( T2) relaxation times measured vs. concentration, temperature, pulse interval (τCPMG) as well as 1H NMR spectral measurements in a wide range of concentrations of bovine serum albumin (B SA ) solutions. The anomalous relaxation behaviour of the water protons, similar to that observed in mammalian lenses, was found in the two most concentrated solutions (44% and 46% ). The functional dependence of the spin-spin relaxation time vs. τCPMG pulse interval and the values of the motional activation parameters obtained from the temperature dependencies of spinlattice relaxation times suggest that the water molecule mobility is reduced in these systems. The slow exchange process on the T2 time scale is proposed to explain the obtained data. The proton spectral measurements support the hypothesis of a slow exchange mechanism in the highest concentrated solutions. From the analysis of the shape of the proton spectra the mean exchange times between bound and bulk water proton groups (τex) have been estimated for the range of the highest concentrations (30% - 46% ). The obtained values are of the order of milliseconds assuring that the slow exchange condition is fulfilled in the most concentrated samples.

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35

Nadig, Gautham, Laura C. Van Zant, Steve L. Dixon i Kenneth M. Merz. "Charge-Transfer Interactions in Macromolecular Systems: A New View of the Protein/Water Interface". Journal of the American Chemical Society 120, nr 22 (czerwiec 1998): 5593–94. http://dx.doi.org/10.1021/ja980564r.

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Rao, Qinchun, Jeancarlo R. Rocca-Smith i Theodore P. Labuza. "Storage stability of hen egg white powders in three protein/water dough model systems". Food Chemistry 138, nr 2-3 (czerwiec 2013): 1087–94. http://dx.doi.org/10.1016/j.foodchem.2012.11.082.

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Polyakov, V. I., O. K. Kireyeva, V. Ya Grinberg i V. B. Tolstoguzov. "Thermodynamic compatibility of proteins in aqueous media. Part. I. Phase diagrams of some water – protein A – protein B systems". Food / Nahrung 29, nr 2 (1985): 153–60. http://dx.doi.org/10.1002/food.19850290210.

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Turov, V. V., P. P. Gorbyk, T. V. Krupska, S. P. Turanska, V. F. Chekhun i N. Yu Luk'yanova. "Composite systems for medical purposes, created on the basis of hydrophobic silica". Surface 13(28) (30.12.2021): 246–75. http://dx.doi.org/10.15407/surface.2021.13.246.

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Composite systems with certain cytotoxic (AM1/lectin) and adsorption (AM1/gelatin) activity have been developed on the basis of methyl silica and protein molecules – lectin and gelatin. For both types of composites, mechanisms of water binding to the surface and methods of transferring of hydrophobic materials into the aquatic environment have been investigated. The state of interfacial water in air, organic and acid media was studied. It has been found that the presence of a hydrophobic component in composites stabilizes of surface water in a weakly associated state, when a significant part of water molecules does not form hydrogen bonds. Liquid hydrophobic medium enhances this effect, and the strong acid (trifluoroacetic), added to it, promotes the transition of water to a strongly associated state. It has been shown that the redistribution of water in the interparticle intervals of AM1 with protein molecules immobilized on their surface changes under the influence of mechanical loads. Mechanoactivated samples are characterized by the possibility of water penetration into the spaces between the primary particles of methyl silica. It has been shown that immobilization of lectin on the surface of AM1 is accompanied by an increase in the interfacial energy gS from 4.1 to 5.2 J/g. This is due to an increase in the concentration of strongly bound water. If we analyze the changes in the distributions of radii R of the clusters of adsorbed water, we can state that in the water adsorbed by native lectin molecules, there are two main maxima at R = 1 and 3 nm. In the immobilized state, the maximum at R = 1 nm is present in both types of water (of different order), but the second maximum is observed only for more ordered associates.

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Nagy, Gabor, Nora Meggyeshazi i Oliver Szasz. "Deep Temperature Measurements in Oncothermia Processes". Conference Papers in Medicine 2013 (2.06.2013): 1–6. http://dx.doi.org/10.1155/2013/685264.

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Temperature in depth of various model systems was measured, starting with muscle and other phantoms. It was shown that the temperature can be selectively increased in the target. In water-protein phantom, the protein coagulation (>60°C) was observed selectively while the water temperature around it was a little higher than room temperature.

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40

Braun, Daniel, Michael Schmollngruber i Othmar Steinhauser. "Towards a complete characterization of the δ-dispersion in dielectric spectroscopy of protein–water systems". Phys. Chem. Chem. Phys. 19, nr 39 (2017): 26980–85. http://dx.doi.org/10.1039/c7cp05216b.

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Zhuravskaya, N. A., E. V. Kikadze, Yu A. Antonov i V. B. Tolstoguzov. "Concentration of proteins as a result of the phase separation of water-protein-polysaccharide systems Part 1. Phase equilibria in water-milk proteins-polysaccharide systems". Food / Nahrung 30, nr 6 (1986): 591–99. http://dx.doi.org/10.1002/food.19860300608.

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STAMATIE, Gabriela Daniela, Denisa Eglantina DUTA, Nastasia BELC, Claudia ZOANI i Florentina ISRAELROMING. "NUTRITIONAL AND FUNCTIONAL PROPERTIES OF SOME PROTEIN SOURCES". AgroLife Scientific Journal 10, nr 1 (30.06.2021): 214–20. http://dx.doi.org/10.17930/agl2021124.

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Nine ingredients protein sources were examined: milk protein, whey protein, Pleurotus mushroom flour, pea protein, corn protein, soy protein, oat protein, hemp protein, sea buckthorn protein in comparison with wheat flour (as control). They were subjected to physicochemical (protein, fat, ash, carbohydrates, aminoacids contents and digestibility) and functional analyzes (water absorption capacity, oil absorption capacity, foaming property and foam stability, gelling property for mixtures of 10% protein ingredient in water, emulsification capacity). The water absorption capacity ranged from 0.54-3.22 WHC. The highest oil absorption capacity was identified for milk protein sample 1.07 WHC (g oil/g sample). The foaming capacity ranged from 0% for hemp protein sample to 91.5% for milk protein sample. The emulsification capacity varied from 69.23% for the corn protein hydrolyzate sample to 54.69% for oat protein sample. Protein ingredients have different functional properties which determine their behaviour in food systems and based on which they can be used in different food applications, for improving the protein content of food products

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Linehan, C. J., D. P. Armstrong, P. T. Doyle i F. Johnson. "A survey of water use efficiency on irrigated dairy farms in northern Victoria". Australian Journal of Experimental Agriculture 44, nr 2 (2004): 131. http://dx.doi.org/10.1071/ea02234.

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Water use efficiency (WUE) in irrigated dairy systems has been defined, in this paper, as the amount of milk (kg milk fat plus protein) produced from pasture per megalitre of water (irrigation plus effective rainfall). A�farm survey was conducted for the 1997–98 and 1998–99 seasons in the Goulburn Irrigation System (GIS) and Murray Irrigation System (MIS) when the irrigation water allocated to irrigators in the GIS was low (100–120% of water right compared with the MIS which was 130 and 200% of water right). These data were analysed in conjunction with information collected on the same farms in the 1994–95 and 1995–96 seasons when the irrigation water allocated to irrigators in both systems was above 150% of water right (Armstrong et al. 1998, 2000). The aim of the survey was to determine if the management decisions made by dairy farmers in seasons of low irrigation water allocations had an impact on WUE.Milk production averaged across the 2 irrigation systems increased significantly over the 5-year period (57 540–75 040 kg milk fat + protein per farm). Over the same period the amount of irrigation water applied (GIS�7.6 ML/ha, MIS 9.2 ML/ha) and the milking area (GIS 72 ha, MIS 73 ha) remained constant. The amount of concentrates fed per cow (GIS 650–1100 kg DM, MIS 480–860 kg DM) and per farm (GIS 119–228 t DM, MIS�72–157 t DM) increased, but pasture consumption (GIS 8.9–9.5 t DM/ha, MIS 9.1–9.7 t DM/ha) did not increase significantly over the survey period. Therefore, the increase in milk production appeared to come primarily from an increase in supplementary feeding rather than an increase in pasture consumption, resulting in no significant change in WUE in either system (GIS 66 kg milk fat + protein/ML, MIS 61 kg milk fat + protein/ML).The survey results indicate that despite varying water allocations in the 2 major irrigation systems in northern Victoria, milk production on farms in both systems increased while changes in WUE could not be detected by the methods used. This suggests tactical options to increase WUE in response to short-term changes in water allocation were either difficult to implement or not a priority in a business sense.

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Liu, Lei, Zhengquan Liu, Peng Huang, Ze Wu i Shuyun Jiang. "Protein-induced ultrathin molybdenum disulfide (MoS2) flakes for a water-based lubricating system". RSC Advances 6, nr 114 (2016): 113315–21. http://dx.doi.org/10.1039/c6ra23786j.

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Protein induced ultrathin MoS₂ flakes were successfully exfoliated, and they were used as additives for water-based lubricating systems, which indicated that they could improve the friction performance and anti-wear abilities at a low concentration.

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Rand, R. P. "Probing the role of water in protein conformation and function". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, nr 1448 (29.08.2004): 1277–85. http://dx.doi.org/10.1098/rstb.2004.1504.

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Life began in a bath of water and has never escaped it. Cellular function has forced the evolution of many mechanisms ensuring that cellular water concentration has never changed significantly. To free oneself of any conceptual distinction among all small molecules, solutes and solvents, means that experiments to probe water's specific role in molecular function can be designed like any classical chemical reaction. Such an ‘osmotic stress’ strategy will be described in general and for an enzyme, hexokinase. Water behaves like a reactant that competes with glucose in binding to hexokinase, and modulates its conformational change and activity. This ‘osmotic stress’ strategy, now applied to many very different systems, shows that water plays a significant role, energetically, in most macromolecular reactions. It can be required to fill obligatory space, it dominates nearest non–specific interactions between large surfaces, it can be a reactant modulating conformational change; all this in addition to its more commonly perceived static role as an integral part of stereospecific intramolecular structure.

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Anderson, J. L. Ross, Ronald L. Koder, Christopher C. Moser i P. Leslie Dutton. "Controlling complexity and water penetration in functional de novo protein design". Biochemical Society Transactions 36, nr 6 (19.11.2008): 1106–11. http://dx.doi.org/10.1042/bst0361106.

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Natural proteins are complex, and the engineering elements that support function and catalysis are obscure. Simplified synthetic protein scaffolds offer a means to avoid such complexity, learn the underlying principles behind the assembly of function and render the modular assembly of enzymatic function a tangible reality. A key feature of such protein design is the control and exclusion of water access to the protein core to provide the low-dielectric environment that enables enzymatic function. Recent successes in de novo protein design have illustrated how such control can be incorporated into the design process and have paved the way for the synthesis of nascent enzymatic activity in these systems.

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De Marco, Iolanda. "Zein Microparticles and Nanoparticles as Drug Delivery Systems". Polymers 14, nr 11 (27.05.2022): 2172. http://dx.doi.org/10.3390/polym14112172.

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Zein is a natural, biocompatible, and biodegradable polymer widely used in the pharmaceutical, biomedical, and packaging fields because of its low water vapor permeability, antibacterial activity, and hydrophobicity. It is a vegetal protein extracted from renewable resources (it is the major storage protein from corn). There has been growing attention to producing zein-based drug delivery systems in the recent years. Being a hydrophobic biopolymer, it is used in the controlled and targeted delivery of active principles. This review examines the present-day landscape of zein-based microparticles and nanoparticles, focusing on the different techniques used to obtain particles, the optimization of process parameters, advantages, disadvantages, and final applications.

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Sun, Qi, Zhenzhen Yang i Xianrong Qi. "Design and Application of Hybrid Polymer-Protein Systems in Cancer Therapy". Polymers 15, nr 9 (8.05.2023): 2219. http://dx.doi.org/10.3390/polym15092219.

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Polymer-protein systems have excellent characteristics, such as non-toxic, non-irritating, good water solubility and biocompatibility, which makes them very appealing as cancer therapeutics agents. Inspiringly, they can achieve sustained release and targeted delivery of drugs, greatly improving the effect of cancer therapy and reducing side effects. However, many challenges, such as reducing the toxicity of materials, protecting the activities of proteins and controlling the release of proteins, still need to be overcome. In this review, the design of hybrid polymer–protein systems, including the selection of polymers and the bonding forms of polymer–protein systems, is presented. Meanwhile, vital considerations, including reaction conditions and the release of proteins in the design process, are addressed. Then, hybrid polymer–protein systems developed in the past decades for cancer therapy, including targeted therapy, gene therapy, phototherapy, immunotherapy and vaccine therapy, are summarized. Furthermore, challenges for the hybrid polymer–protein systems in cancer therapy are exemplified, and the perspectives of the field are covered.

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Halle, Bertil. "Protein hydration dynamics in solution: a critical survey". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, nr 1448 (29.08.2004): 1207–24. http://dx.doi.org/10.1098/rstb.2004.1499.

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The properties of water in biological systems have been studied for well over a century by a wide range of physical techniques, but progress has been slow and erratic. Protein hydration—the perturbation of water structure and dynamics by the protein surface—has been a particularly rich source of controversy and confusion. Our aim here is to critically examine central concepts in the description of protein hydration, and to assess the experimental basis for the current view of protein hydration, with the focus on dynamic aspects. Recent oxygen–17 magnetic relaxation dispersion (MRD) experiments have shown that the vast majority of water molecules in the protein hydration layer suffer a mere twofold dynamic retardation compared with bulk water. The high mobility of hydration water ensures that all thermally activated processes at the protein–water interface, such as binding, recognition and catalysis, can proceed at high rates. The MRD–derived picture of a highly mobile hydration layer is consistent with recent molecular dynamics simulations, but is incompatible with results deduced from intermolecular nuclear Overhauser effect spectroscopy, dielectric relaxation and fluorescence spectroscopy. It is also inconsistent with the common view of hydration effects on protein hydrodynamics. Here, we show how these discrepancies can be resolved.

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Hudori, Hudori, Toshiro Yamada, Yukitaka Suzuki, Maulana Yusup Rosadi, Hiroto Tamaoki i Fusheng Li. "Characterization of dissolved organic matter at a water treatment plant with closed systems in different seasons". Water Supply 20, nr 5 (3.06.2020): 2013–20. http://dx.doi.org/10.2166/ws.2020.117.

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Abstract This research focuses on characterizing the dissolved organic matter found at water treatment plants with closed systems. Recycled water generated as a by-product of water treatment is added to raw water in those systems. The dissolved organic matter in the raw water was found to be higher in summer than in winter, but the water treatment process was able to produce purified water of the similar quality in both seasons. The recycled water contained mostly low molecular weight and protein-like substances, and this composition was different from that of the raw water, which mainly contained humic-like substances. The recycled water did not influence the concentration of humic-like substances or the molecular weight distribution in the influent water.

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