Water in Biology, Chemistry and Physics

Robinson, Gina; Singh, Surjit; Zhu, S.‐B.; Evans, M. W.

doi:10.1142/9789812796981

Cited by 122 publications

(139 citation statements)

References 0 publications

Supporting

Mentioning

137

Contrasting

Order By: Relevance

“…Effectively, water is a transiently-connected network of molecules with something like 75% of all molecules in room temperature liquid connected to three-or-four nearest neighbors [165, 168]. At approximately 2 kJ/mole (0.5 kCal/mole) of hydrogen bonds in liquid water [169], there is a strong energetic preference for the self associated state due to hydrogen bonding (which can be treated as a partially electrostatic and partially chemical Lewis acid/base (AB) interaction [14]).…”

Section: 0 Technical Backgroundmentioning

confidence: 99%

Protein adsorption in three dimensions

2012

View full text Add to dashboard Cite

Recent experimental and theoretical work clarifying the physical chemistry of blood-protein adsorption from aqueous-buffer solution to various kinds of surfaces is reviewed and interpreted within the context of biomaterial applications, especially toward development of cardiovascular biomaterials. The importance of this subject in biomaterials surface science is emphasized by reducing the “protein-adsorption problem” to three core questions that require quantitative answer. An overview of the protein-adsorption literature identifies some of the sources of inconsistency among many investigators participating in more than five decades of focused research. A tutorial on the fundamental biophysical chemistry of protein adsorption sets the stage for a detailed discussion of the kinetics and thermodynamics of protein adsorption, including adsorption competition between two proteins for the same adsorbent immersed in a binary-protein mixture. Both kinetics and steady-state adsorption can be rationalized using a single interpretive paradigm asserting that protein molecules partition from solution into a three-dimensional (3D) interphase separating bulk solution from the physical-adsorbent surface. Adsorbed protein collects in one-or-more adsorbed layers, depending on protein size, solution concentration, and adsorbent surface energy (water wettability). The adsorption process begins with the hydration of an adsorbent surface brought into contact with an aqueous-protein solution. Surface hydration reactions instantaneously form a thin, pseudo-2D interface between the adsorbent and protein solution. Protein molecules rapidly diffuse into this newly-formed interface, creating a truly 3D interphase that inflates with arriving proteins and fills to capacity within milliseconds at mg/mL bulk-solution concentrations CB. This inflated interphase subsequently undergoes time-dependent (minutes-to-hours) decrease in volume VI by expulsion of either-or-both interphase water and initially-adsorbed protein. Interphase protein concentration CI increases as VI decreases, resulting in slow reduction in interfacial energetics. Steady-state is governed by a net partition coefficient P=true(/CBCItrue). In the process of occupying space within the interphase, adsorbing protein molecules must displace an equivalent volume of interphase water. Interphase water is itself associated with surface-bound water through a network of transient hydrogen bonds. Displacement of interphase water thus requires an amount of energy that depends on the adsorbent surface chemistry/energy. This “adsorption-dehydration” step is the significant free-energy cost of adsorption that controls the maximum amount of protein that can be adsorbed at steady state to a unit adsorbent-surface area (the adsorbent capacity). As adsorbent hydrophilicity increases, protein adsorption monotonically decreases because the energetic cost of surface dehydration increases, ultimately leading to no protein adsorption near an adsorbent water wettability (surface energy) characterized ...

show abstract

Section: 0 Technical Backgroundmentioning

confidence: 99%

Protein adsorption in three dimensions

2012

View full text Add to dashboard Cite

show abstract

“…Water has some properties that distinguish it from simpler liquids. [1–5] Some of the most important anomalies of pure water are the following: maximum density at 4 °C in the liquid phase, negative coefficient of thermal expansion below that temperature, high surface tension and viscosity, a minimum in the isothermal compressibility, and a large heat capacity. Used as a solvent, water also has many unusual properties: for nonpolar solutes, a large entropy opposes solvation at room temperature, and a large heat capacity of transfer of apolar solvent into water.…”

Section: Introductionmentioning

confidence: 99%

Ions increase strength of hydrogen bond in water

Urbič¹

2014

Chemical Physics Letters

View full text Add to dashboard Cite

Knowledge of water-water potential is important for an accurate description of water. Potential between two molecules depends upon the distance, relative orientation of each molecule and local environment. In simulation, water-water hydrogen bonds are handled by point-charge water potentials and by polarizable models. These models produce good results for bulk water being parameterized for such environment. Water around surfaces and in channels, however is different from bulk water. Using quantum-mechanical methods, hydrogen bond strength was calculated in the vicinity of different monoions. A simple empirical relationship was discovered between the maximum hydrogen bond and the electric field produced by ion.

show abstract

“…The analytical forms of these potentials were fitted to the calculated energy surfaces details of these potentials are given in ref. (Robinson et al, 1996). This resulted in unusually long O-O distances and relative soft curvatures at the potential minima and made these models less successful in simulating the bulk properties of water and ice (Dong et al, 2001a).…”

Section: Water-water Potentialsmentioning

confidence: 99%

“…These properties give water and ice a number of 'abnormal properties', which can not be explained by the 'ordinary rules' of physics and chemistry. As a consequence, a large number of models have been proposed in attempts to interpret some of these properties of water such as water' s high heat capacity, high melting and boiling temperature, and its density and entropy fluctuations (see reviews by Frank, 1972;Eisenberg et al, 1972;Robinson et al, 1996). Meanwhile, a significant number of water potentials have also been Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Neutron scattering and computer simulation studies of ice dynamics

Dong

2002

J Ocean Univ. China

View full text Add to dashboard Cite

In this article we describe a range of simulations (lattice dynamics and molecular dynamics) of the inelastic incoherent neutron scattering spectra of ices (normal ice, ice lI and ice N ). These simulations use a variety of different intermolecular potentials from simple classic pair-wise (rigid and non-rigid molecule) potentials to sophisticated polarisable potentials. It was found that MCY makes stretching and bending interactions too weak while others do them well. We demonstrate that in order to reproduce the measured neutron spectrum, greater anisotropy (or orientational variation) is required than these potentials presently provide. tion and Raman scattering. These are very powerful techniques, which have been highly refined, and their usage has resulted in extensive and valuable data for ice (Li et al., 1992;Li et al., 1991). For ice, however, the normal selection rules governing the interaction of radiation with matter are broken due to the local structural disorder (or proton disordering in crystalline structures of ice), and analysis of the spectral intensities is in general difficult. On the other hand, although IR and Raman spectra are very sensitive to the intramolecular modes involving the O-H stretching and bending, they are less sensitive to the intermolecular modes involving the vibrations of water molecules against each other. Therefore, under normal circumstances, optical spectroscopy provides only limited data in the translational region which is vitally important for us to obtain direct information about the hydrogen bond interaction. In contrast, Inelastic Neutron Scattering (INS) spectroscopy is a more powerful probe, its results are directly proportional to Phonon Density of States (PDOS), INS provides an excellent opportunity for the construction and testing potential functions. Because optical selection rules are not involved, INS measures all modes (IR/Raman measure the modes at the Brillouin Zone q -0) and is particularly suitable for studying disordered systems. It provides direct information on the hydrogen bond interactions in ice.

show abstract

Water in Biology, Chemistry and Physics

Cited by 122 publications

References 0 publications

Protein adsorption in three dimensions

Protein adsorption in three dimensions

Ions increase strength of hydrogen bond in water

Neutron scattering and computer simulation studies of ice dynamics

Contact Info

Product

Resources

About