Science question - proteins?

Question

doing an assignment on casien and albium and i need to describe how the differenct structures of the two account for the differences in soluability....

i it to do with secondary, tertiary stucture etc???

if yes how so?

Answer 1

Casein is a protein that is made up largely of proline, and uncharged, non-polar protein. Because of this it lacks a secondary structure and tertiary structure which are common to other proteins. Since it is largely uncharged and non-poar it does not interact with H20 to become soluble, thus they are hydrophobic.

Albumin, is actually a large category of proteins defined by their ability to become soluble in water. This is because of their globular structure. Globular (a somewhat dated term for proteins) means that they are spherical. This means that they have a secondary and tertiary structure. This is due to the interactions between the hydrophobic and hydrophilic portions of the protein. The hydrophoblic portion of the proteins tend to be found at the centre of the sphere, while the hydrophilic potions tend to be found on the outside of the sphere. This structure allows dipole-dipole moments with H20 allowing the protein to become more or less soluble in water.