Physical Chemistry of Foods

it may be that such conformations cannot be reached because of the intricacies of the folding process. It is by no means certain ...

Transitions with the native state are slow and cooperative, those with the unfolded state fast and noncooperative. Characteristi ...

which does not have a double-bond character, implying that rotation about the 22 CO 22 N<bond is possible; trans and cis conf ...

preventing return to the native state. This is far less likely at low temperature. Kinetic aspects are discussed in Section 7.2. ...

nate, have a strong destabilizing effect, acting even at room temperature (Figure 7.7b). Manyneutralsolutes also have a distinct ...

bonds. The overall result mostly is loss of the native conformation, but not formation of a highly unfolded state. Several sugar ...

whereKis the equilibrium value of½NŠ/½UŠandVis total molar volume of the system. Since a very high pressure is needed to cause u ...

conformational stability is less, and if the adsorbent is more hydrophobic, presumably because the driving force for conformatio ...

Question Can you explain why bringing an aqueous solution of a globular protein into a shear field, shear rate 10^4 s
^1 , would ...

Unfolding Kinetics. Figure 4.5 gives an example (the enzyme alkaline phosphatase) of kinetic parameters for protein denaturation ...

Irreversibility. The reasoning given above is also an oversimplification in another sense. Most of the results discussed concern ...

where I stands for ‘‘inactive’’ or ‘‘irreversibly changed’’ form. If, moreover, all reactions were first order, the rate of chan ...

ForT 4 Tden;K 4 1, andkobs&ki, and the latter probably has a weak temperature dependence as compared to ku.AtT 5 Tden;K 5 1, ...

The reaction U?I may not be first order, butsecond order. A case in point is aggregation of unfolded protein, which is rather c ...

It may finally be recalled that conditions during heating, such as pH and ionic composition, greatly influence denaturation rate ...

The solubility of proteins in aqueous media is widely variable, from virtually zero to about 35%by volume. Both protein composit ...

Salting In. The effect ofelectrostatic interactionson solubility can be derived from the Debye–Hu ̈ckel theory, which is briefly ...

indeed what is observed for fairly hydrophilic globular proteins; an example is in Figure 7.12. The increase in solubility by in ...

Salting Out. Many proteins are fairly hydrophobic, several seed storage proteins, for example, such as those from soya beans. Mo ...

increase the conformational stability of globular proteins (Section 7.2.2) generally decrease their solubility; compare Figures ...