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Sulfate-binding proteins

Saito, A., Munakata, H., and Satoh, K. (2002) Glyco-westem blotting biotinylated dermatan sulfate as a probe for the detection of dermatan sulfate binding proteins using western blotting. Connect Tissue Res 43, 1-7. [Pg.130]

Pflugrath, J. W., Quiocho, F. A., The 2-a resolution structure of the sulfate-binding protein involved in active-transport in salmonella-typhimurium. Journal of Molecular Biology 1988, 200, 163-180. [Pg.316]

Pflugrath JW, Quiocho FA (1985) Sulfate sequestered in the sulfate-binding protein of salmonella-typhimurium is bound solely by hydrogen-bonds. Nature 314 257-260... [Pg.214]

Fig. 15. Polypeptide folding patterns for (a) one-half of a transferrin molecule (the N-lobe of lactoferrin) and (b) the bacterial periplasmic sulfate-binding protein. Adapted from Baker et al. (85), with permission. Fig. 15. Polypeptide folding patterns for (a) one-half of a transferrin molecule (the N-lobe of lactoferrin) and (b) the bacterial periplasmic sulfate-binding protein. Adapted from Baker et al. (85), with permission.
Fig. 16. Comparison of the anion binding sites in lactoferrin (left) and the bacterial sulfate-binding protein (right). From Baker et al. (82), with permission. Fig. 16. Comparison of the anion binding sites in lactoferrin (left) and the bacterial sulfate-binding protein (right). From Baker et al. (82), with permission.
Free-Energy Changes for the Introduction of a Water Molecule into Pure Water and into Two Cavities in Sulfate-Binding Protein (SBP) ... [Pg.194]

An example of this kind of calculation, due to Wade et al., is the computation of the hydration of two internal cavities in a sulfate-binding protein. The results are given in Table 2.30. The main difference between having a dry cavity and having a wet one is the hydration bond energy. [Pg.194]

Figure 4. Schematic diagram of the hydrogen bonds from the sulfate-binding protein (SBP) to the bound sulfate. Figure 4. Schematic diagram of the hydrogen bonds from the sulfate-binding protein (SBP) to the bound sulfate.
Amides, bearing both H-bond acceptors (C=0) and donors (NH), play an important role in Namre (e.g., a helices and sheets of peptides and proteins, ion channels), and in technology as structural materials (e.g.. Nylons) [4]. For example, the X-ray crystal structure of the sulfate-binding protein of Salmonella typhimurium shows that the sulfate is bound by seven H-bonds, five of which involve amide NH groups of polypeptides [5]. The pXa of the amide NH is about 12-21 and becomes lower when modified with electron-deficient groups. Consequentiy, amide as an excellent H-bond donor to bind anionic species has attracted much attention of supramo-lecular, biological, and environmental chemists, especially for anion recognition, transport, and pollution remediation [6-11]. [Pg.138]


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See also in sourсe #XX -- [ Pg.228 ]

See also in sourсe #XX -- [ Pg.228 ]

See also in sourсe #XX -- [ Pg.206 ]




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