Question

hydrophobicity is important to an amino acids beacuse
A. It determines the unique sequence of mRNA
B. It determines the function of the protein
C.It determines the shape of the protein
D. It is only important when the coding region on the DNA is an exon

If you could a source would be extremely helpfull!

Answer 1

The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules.[1][2] The name, literally meaning "water-fearing," describes the segregation and apparent repulsion between water and nonpolar substances. The hydrophobic effect explains the separation of a mixture of oil and water into its two components, and the beading of water on nonpolar surfaces such as waxy leaves. At the molecular level, the hydrophobic effect is important in driving protein folding,[3][4] formation of lipid bilayers and micelles, insertion of membrane proteins into the nonpolar lipid environment and protein-small molecule interactions.[5] Substances for which this effect is observed are known as hydrophobes.

Source: http://en.wikipedia.org/wiki/Hydrophobic_effect

In biochemistry, the hydrophobic effect can be used to separate mixtures of proteins based on their hydrophobicity. Column chromatography with a hydrophobic stationary phase such as phenyl-sepharose will cause more hydrophobic proteins to travel more slowly, while less hydrophobic ones elute from the column sooner. To achieve better separation, a salt may be added (higher concentrations of salt increase the hydrophobic effect) and its concentration decreased as the separation goes on.

Source: http://en.wikipedia.org/wiki/Hydrophobic_effect

Amino acids are grouped according to what their side chains are like. The nine amino acids that have hydrophobic side chains are glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp). Shown at the right is the structure of valine. These side chains are composed mostly of carbon and hydrogen, have very small dipole moments, and tend to be repelled from water. This fact has important implications for proteins' tertiary structure (see the Proteins 2 module for a discussion of tertiary structure).

Source: http://www.chem.wisc.edu/deptfiles/genchem/netorial/modules/biomolecules/modules/protein1/prot13.htm