Which group of amino acids would be preferentially found in the interior of a gl

Question

Which group of amino acids would be preferentially found in the interior of a globular protein? (Circle only oneX5 pts 2. i. Aspartic acid, Glutamic acid ii. Lysine, Histidine ili. Isoleucine, Valine iv. Serine, Asparagine Which group of amino acids contains polar hydroxyl groups in their structures? (Circle only one) 15 pts] i. Arginine, Histidine i. Phenylalanine, Tryptophan ii. Glycine, Alanine iv. Serine, Threonine Match the protein order with the appropriate characteristics given in questions 5-9. 15 pts) A. Quaternary structure B. Tertiary structure C. Secondary structure D. Primary structure 4. Subunits interactions as they occur between the and subunits of hemoglobin 5. -helix and -sheet 6. Hydrophobic interactions drive folding of the polypeptide chain into a fully-folded protein 7· Burns used to reverse the direction of the polypeptide chain, 8, Bond between an amino acid amino group and an adjacent amino acid carboxyl group

Explanation / Answer

(1) As in all proteins, the primary structure of globular proteins consists of a polypeptide, or chain of amino acids joined via peptide bonds. Hydrogen bonds between carboxyl and amine groups of the amino acids contribute to the secondary structure, which in globular proteins may include alpha-helices, beta-sheets, or both. Globular proteins are folded such that their tertiary structure consists of the polar, or hydrophilic, amino acids arranged on the outside and the nonpolar, or hydrophobic, amino acids on the inside of the three-dimensional shape. This arrangement is responsible for the solubility of globular proteins in water. So, non polar Amino Acids being, Isoleucine and Valine is correct choice. Ans (iii)

Ans (2)

Serine, Threonine, and Tyrosine - Polar Amino Acids With a Hydroxyl Group Ans (iv)

This allows these amino side chains to form hydrogen bonds which play an important role in protein structure and funtion. They hydroxyl is also a reactive functional group and can form covalent bonds to other substituents that may modify the protein struture, such as the oligosaccharide of glycoproteins and the phosphate of regulated enzymes.

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