Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties

Edsall, John T.; McKenzie, H.A.

doi:10.1016/0065-227x(83)90008-4

Cited by 206 publications

(50 citation statements)

References 185 publications

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“…This is equivalent to a molar ratio of 15 water molecules per amino acid residue. As water is withdrawn during dehydration, the hydration will be reduced and the orientation of the various amino groups and the configuration of the looped protein will be altered [13]. The optimum arrangement will also be affected by the ionic charges arising from the concentration of the mineral ions.…”

Section: Bonding Of Proteinsmentioning

confidence: 99%

Insolubility of milk powder products – A minireview

Baldwin

2010

Dairy Sci. Technol.

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-In this paper, the formation of insolubility in milk powder is described, and the factors affecting the reaction are discussed. The zone in which casein proteins are most sensitive to heat is in the moisture range that occurs during spray drying. The rate of reaction has been determined and shows differences of orders of magnitude with the moisture content. The effect of chemical reagents on the extent of reaction gives insights into the chemical bonds that inhibit hydration. Information on the drying of casein products and individual proteins is used to infer that the withdrawal of moisture from casein proteins and the concentration of divalent cations during drying lead to alterations in the conformation of proteins that have an adverse effect on their rehydration during reconstitution. Further work to fully characterise these effects is required.spray drying / powder / casein / insolubility / kineticsRésumé -Insolubilité des poudres laitières -une mini-revue. L'apparition de l'insolubilité des poudres laitières est décrite et les facteurs affectant cette réaction sont discutés dans cet article. La zone dans laquelle les caséines sont les plus sensibles à la chaleur se situe dans la gamme d'humidité intervenant au cours du procédé de séchage par atomisation. La vitesse de réaction a été déterminée et montre des différences d'ordres de grandeur des taux d'humidité. L'effet des réactifs chimiques sur l'étendue de la réaction donne un aperçu des liaisons chimiques qui inhibent l'hydratation. On peut déduire de l'information obtenue sur le séchage des caséines et des protéines individuelles que l'élimination de l'humidité des caséines et la concentration en cations divalents au cours du séchage conduisent à des modifications de la conformation des protéines qui peuvent avoir des effets négatifs sur leur réhydratation au cours de la reconstitution des poudres. Un travail ultérieur est nécessaire pour caractériser complètement ces effets.séchage par atomisation / poudre / caséine / insolubilité / cinétique

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Section: Bonding Of Proteinsmentioning

confidence: 99%

Insolubility of milk powder products – A minireview

Baldwin

2010

Dairy Sci. Technol.

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“…Since the number (N I ) of internal water molecules shows large (relative) variations (not directly correlated with N S or surface area) among different proteins (Finney, 1979;Edsall & McKenzie, 1983;Baker & Hubbard, 1984;Rashin et al, 1986;Meyer, 1992), we expect a correspondingly large variation of the ratio b/a. In particular, b/a should be much larger for BPTI, which contains four buried water molecules in all three investigated crystal forms (Deisenhofer & Steigemann, 1975;Wlodawer et al, 1984Wlodawer et al, , 1987a as well as in solution (Otting & Wü thrich, 1989;Otting et al, 1991a), than for ubiquitin, the crystal structure of which does not reveal any internal water molecules (Vijay-Kumar et al, 1987).…”

Section: Internal Watermentioning

confidence: 99%

Protein Hydration Dynamics in Aqueous Solution: A Comparison of Bovine Pancreatic Trypsin Inhibitor and Ubiquitin by Oxygen-17 Spin Relaxation Dispersion

Денисов

Halle

1995

Journal of Molecular Biology

162

177

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Water oxygen-17 spin relaxation was used to study hydration and dynamics Condensed Matter Magnetic Resonance Group, Chemical of the globular proteins bovine pancreatic trypsin inhibitor (BPTI) and ubiquitin in aqueous solution. The frequency dispersion of the longitudinal Center, Lund University P. O. Box 124, S-22100 Lund and transverse relaxation rates was measured over the Larmor frequency Sweden range 2.6 to 49 MHz in the pD range 2 to 11 at 27°C. While the protein-induced relaxation enhancement was similar for the two proteins at high frequencies, it was an order of magnitude smaller for ubiquitin than for BPTI at low frequencies. This difference was ascribed to the abscence, in ubiquitin, of highly ordered internal water molecules, which are known to be present in BPTI and in most other globular proteins. These observations demonstrate that the water relaxation dispersion in protein solutions is essentially due to a few structural water molecules buried within the protein matrix, but exchanging rapidly with the external water. The relaxation data indicate that the internal water molecules of BPTI exchange with bulk water on the time-scale 10 −8 to 10 −6 second thus lowering the recently reported upper bound on the residence time of these internal water molecules by four orders of magnitude, and implying that local unfolding occurs on the submicrosecond time-scale. The water molecules residing at the surface of the two proteins were found to be highly mobile, with an average rotational correlation time of approximately 20 picoseconds. For both proteins, the oxygen-17 relaxation depended only very weakly on pD, showing that ionic residues do not perturb hydration water dynamics more than other surface residues. We believe that the present results resolve the long-standing controversy regarding the mechanism behind the spin relaxation dispersion of water nuclei in protein solutions, thus establishing oxygen-17 relaxation as a powerful tool for studies of structurally and functionally important water molecules in proteins and other biomolecules.

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“…The solvent environment surrounding a protein is generally divided into two classes: ( I ) bulk water that is fluid and not bound to the protein, and (2) water that is either partially or strongly bound (Edsall & McKenzie, 1983: Otting et al, 1991Badger, 1993;Levitt & Park, 1993;Ringe, 1995). A typical method for analyzing the contributions of bound solvent is to use molecular graphics to visualize the water bound in a single protein structure, or a small number of closely related structures, and their proximity to catalytic or ligand-binding residues.…”

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confidence: 99%

Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity

Sanschagrin

Kuhn

1998

Protein Science

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Cluster analysis is presented as a technique for analyzing the conservation and chemistry of water sites from independent protein structures, and applied to thrombin, trypsin, and bovine pancreatic trypsin inhibitor (BPTI) to locate shared water sites, as well as those contributing to specificity. When several protein structures are superimposed, complete linkage cluster analysis provides an objective technique for resolving the continuum of overlaps between water sites into a set of maximally dense microclusters of overlapping water molecules, and also avoids reliance on any one structure as a reference. Water sites were clustered for ten superimposed thrombin structures. three trypsin structures, and four BPTI structures. For thrombin, 19% of the 708 microclusters, representing unique water sites, contained water molecules from at least half of the structures, and 4% contained waters from all 10. For trypsin, 77% of the 106 microclusters contained water sites from at least half of the structures, and 57% contained waters from all three. Water site conservation correlated with several environmental features: highly conserved microclusters generally had more protein atom neighbors, were in a more hydrophilic environment, made more hydrogen bonds to the protein, and were less mobile. There were significant overlaps between thrombin and trypsin conserved water sites, which did not localize to their similar active sites, but were concentrated in buried regions including the solvent channel surrounding the Na' site in thrombin, which is associated with ligand selectivity. Cluster analysis also identified water sites conserved in thrombin but not trypsin, and vice versa, providing a list of water sites that may contribute to ligand discrimination. Thus, in addition to facilitating the analysis of water sites from multiple structures, cluster analysis provides a useful tool for distinguishing between conserved features within a protein family and those conferring specificity.

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Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties

Cited by 206 publications

References 185 publications

Insolubility of milk powder products – A minireview

Insolubility of milk powder products – A minireview

Protein Hydration Dynamics in Aqueous Solution: A Comparison of Bovine Pancreatic Trypsin Inhibitor and Ubiquitin by Oxygen-17 Spin Relaxation Dispersion

Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity

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