Which amino acids in the wool protein have groups that are affected by the changes in pH?
Proteins are composed of long chains of amino acids, which coil up on themselves due to hydrogen bonding and other intermolecular forces. Most protein textiles are derived from structural proteins produced by animals, in particular wool and silk.
Wool is largely composed of the same protein as your nails and hair keratin.
Proteins contain two major functional groups which affect their ability to interact with dyes: -NH2 which can protonated to form a positively charged group, and -COOH, which can be deprotonated to form a negatively charged group.
Changes in pH change the attractions between the groups in the side chains of the protein. The interactions between the side chains of the amino acids determine the shape of a protein.
Four types of attractive interactions determine the shape and stability of a protein. The two that pH changes affect are salt bridges (a) and hydrogen bonding (b).
Salt Bridges
Salt bridges are ionic bonds between positively and negatively charged side chains of amino acids. An example is the attraction between a -COO- ion of lysine and an -NH+3 ion of aspartic acid.
Increasing the pH by adding a base converts the -NH+3 ion to a neutral -NH2 group.
Decreasing the pH by adding an acid converts the –COO- ion to a neutral -COOHgroup.
In each case the ionic attraction disappears, and the protein shape unfolds.
Hydrogen Bonding
Various amino acid side chains can hydrogen bond to each other. Examples are:
• Two alcohols: Ser, Thr, and Tyr.
• Alcohol and amine: Ser and Lys
• Alcohol and amide: Ser and Asn
• Alcohol and acid: Asp and Tyr
• Two acids: Asp and Glu
Changing the pH disrupts the hydrogen bonds, and this changes the shape of the protein.
Which amino acids in the wool protein have groups that are affected by the changes in...
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