Protein hydration water

Membranes such as NC supported on glass may be more applicable for protein microarrays than glass substrates. Supported charged nylon membranes for microarrays are currently entering the marketplace as well. The essential ingredient for protein is water. Protein hydration reduces the likelihood for surface denaturation. Hydrophilic membranes allow proteins to... 

Z1, P Cieplak, W D Cornell and P A Kolhnan 1993. A Well-Behaved Electrostatic Potential Based 5thod for Deriving Atomic Charges - The RESP Model. Journal of Physical Chemistry 97 10269-10280. sen H C, J P M Postma, W F van Gunsteren and J Hermans 1981. Interaction Models for Water in lation to Protein Hydration. In Pullman B (Editor). Intermolecular Forces. Dordrecht, Reidel, I. 331-342. 

HJC Berendsen, JPM Postma, WE van Gunsteren, J Hermans. Interaction models of water m relation to protein hydration. In B Pullman, ed. Intermolecular Eorces. Dordrecht, Holland Reidel, 1981, pp 331-341. 

The information obtained from X-ray measurements on the arrangement of the water molecules naturally depends very much on the resolution and state of refinement of the crystal structure investigated. For detailed information on the organization of water molecules in the protein hydration shell at the surface and on the bulk water in the crystals a 1,2 to 1,8 A resolution range is necessary 153>. 

Li TP, Hassanali AAP, Kao YT, Zhong DP, Singer SJ (2007) Hydration dynamics and time scales of coupled water-protein fluctuations. J Am Chem Soc 129(11) 3376-3382... 

Initial screening conditions are suggested in Table 6.1. Multiple pH values are included because mobile-phase pH can significantly affect retention. Major selectivity shifts such as transpositions in elution order are fairly common changes in resolution are much more so.2,14-16 Changes in retention due to pH variation relate to protein hydration. Proteins are minimally charged at their isoelectric points (pis). This means that they carry the minimum of electrostricted hydration water. Both protein surface hydrophobicity and HIC retention should therefore reach their maximum at a protein s pi.6 As pH is either increased or... 

Other than water, protein is the major constituent of meat averaging nearly 21% in heef or chicken meat, with fat varying fiom 4.6 to 11.0% in beef and fiom 2.7 to 12.6% in chickoi. The principal radiolytic reactions of aqueous solutions of aliphatic amino acids are reductive deamination and decarboxylation. Alanine yields NH3, pyruvic add, acetaldehyde, propionic acid, CO2, H2, and ethylamine (6). Sulfur-containing amino adds are espedally sensitive to ionizing radiation. Cysteine can be oxidized to cystine by the hydroxyl radical or it can react with the hydrated electron and produce... 

Water molecules are oriented at the surfaces of macromolecules as well as at solid surfaces. For example, Bernal (1965) refers to a regular formation of ice surrounding most protein molecules, although by ice he does not mean free water ice. Bound water in hydration shells surrounding macromolecules in aqueous solutions is sometimes denoted as lattice-ordered or ice-like and has been taken into account in interpreting the dielectric functions of such solutions (Buchanan et al., 1952 Jacobson, 1955 Pennock and Schwan, 1969). 

In sharp contrast to the large number of experimental and computer simulation studies reported in literature, there have been relatively few analytical or model dependent studies on the dynamics of protein hydration layer. A simple phenomenological model, proposed earlier by Nandi and Bagchi [4] explains the observed slow relaxation in the hydration layer in terms of a dynamic equilibrium between the bound and the free states of water molecules within the layer. The slow time scale is the inverse of the rate of bound to free transition. In this model, the transition between the free and bound states occurs by rotation. Recently Mukherjee and Bagchi [14] have numerically solved the space dependent reaction-diffusion model to obtain the probability distribution and the time dependent mean-square displacement (MSD). The model predicts a transition from sub-diffusive to super-diffusive translational behaviour, before it attains a diffusive nature in the long time. However, a microscopic theory of hydration layer dynamics is yet to be fully developed. 

Water retention Brix measurement for by hydrometer, 31 -32 method reliability, 32-33 by refractometer, 30-31 protein hydration properties, 295 (table) Water gravimetric measurement by drying, 4-11... 

During ageing of the mix, interfacial milk protein hydration also increases simultaneously with protein desorption from the fat globules. The water content of the isolated cream layers after centrifugation of ice cream mix can be analyzed by Karl Fischer titration. From such analyses, interfacial protein hydration can be calculated (Figure 13). 

The voluminosity or hydration of interfacially bound protein may be calculated from the amount of water bound per gram of fat divided by the amount of protein bound per gram of fat. This corresponds to the volume of water per gram interfacial protein. Calculations show that emulsifiers facilitate interfacial protein hydration. This property is probably connected with their ability to desorb protein from the interface (Figure 14). 

Both internal structure and overall size and shape of proteins vary enormously. Globular proteins vary considerably in the tightness of packing and the amount of internal water of hydration. However, a density of 1.4 g cm-3 is typical. 

Fig. 7. Schematic representation of AMDH solution structures. The active structures have two parts a catalytically active core, conceivably similar to that in non-halophilic MDH, and protruding loops, required for stabilization in KCl, NaCl, and MgCl2 solvents. In potassium phosphate the protein dimer is stabilized by the hy-drophobicity of the core and the protruding loops are disordered. In KCl (or NaCl) the protein is stabilized by the interaction of the loops in a specific protein—water-salt hydration network. In MgCl2 a similar structure exists with the same amount of water molecules coordinated by fewer salt ions. In low salt concentration, the protein is unfolded and its hydration is like that of nonhalophilic proteins. From Zaccai el al. (1989), with permission.

Berendsen HJ, Postma JP, van Gunsteren WF, Hermans J (1981) Interaction models for water in relation to protein hydration. In Pullman B (ed) Intermolecular forces. D. Reidel, Dordrecht, pp 331-342... 

HYDRATION DYNAMICS AND COUPLED WATER-PROTEIN FLUCTUATIONS PROBED BY INTRINSIC TRYPTOPHAN... 

Molecular dynamics (MD) simulations [29-31], coupled with experimental observations, have played an important role in the understanding of protein hydration. They predicted that the dynamics of ordered water molecules in the surface layer is ultrafast, typically on the picosecond time scales. Most calculated residence times are shorter than experimental measurements reported before, in a range of sub-picosecond to 100 ps. Water molecules at the surface are very mobile and are in constant exchange with bulk water. For example, the trajectory study of myoglobin hydration revealed that among 294 hydration sites, the residence times at 284 sites (96.6% of surface water molecules) are less than lOOps [32]. Furthermore, the population time correlation functions... 

Femtosecond spectroscopy has an ideal temporal resolution for the study of ultrafast water motions from femtosecond to picosecond time scales [33-36]. Femtosecond solvation dynamics is sensitive to both time and length scales and can be a good probe for protein hydration dynamics [16, 37-50]. Recent femtosecond studies by an extrinsic labeling of a protein with a dye molecule showed certain ultrafast water motions [37-42]. This kind of labeling usually relies on hydrophobic interactions, and the probe is typically located in the hydrophobic crevice. The resulting dynamics mostly reflects bound water behavior. The recent success of incorporating a synthetic fluorescent amino acid into the protein showed another way to probe protein electrostatic interactions [43, 48]. 

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