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Fig. 8. The electrostatic potential of the electron density map of the whole P0 protein. The
electrostatic potential is calculated using the Coulomb algorithm implemented in
SwissPDBViewer. Adjusted variables for the algorithm are: dielectric constant of solvent
equal ε=80.0; dielectric constant of protein ε=4.0; solvent ionic strength 5.0 mM. Blue
signifies positive charge and red, negative charge. The range of the mesh depends on the
strength of the electrostatic potential of the analyzed region.
hydrophobic residues. P0_Int is strongly hydrophilic and rich in basic
amino acids: Arg and Lys; the average pI of P0_Int is more than 10 (Fig.
8, Table 1). This part contains a short, strongly hydrophobic region, but its
hydrophobic nature is reduced by the charged surroundings. The spatial
structure of the P0_Int part is sensitive to changes in physical-chemical
solvent properties (Wong, Filbin, 1994; Luo et al ., 2007).
Structural Effects of Breaking the Disulfide Bridge
The P0 protein contains only one disulfide bridge, which is located in the
central part of the P0_Ex subunit between 21 Cys-S—S- 98 Cys. This disulfide
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