Biochem Lec 1 - AAs and Protein Structure

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Biochem Lec 1 - AAs and Protein Structure
2011-09-11 19:20:23
Block Biochem Lecture

Biochem - Block 2 - Lecture 1 - Amino Acids and Protein Structure
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  1. Why is the -OH on tyrosine important?
    The –OH on tyrosine is important because it can be phosphorylated by tyrosine kinases, which are important regulatory enzymes responding to growth factors. Several recently developed cancer drugs [imatinib (Gleevac), sunitinib (Sutent), sorafenib (Nexavar), & several more] are inhibitors of tyrosine kinases.
  2. Describe the native structure of a protein and how AA are arranged within it
    Proteins spontaneously fold into a unique three dimensional (3D) structure (native structure) that almost always represents the lowest free energy of all possible folding patterns. In a properly folded protein, apolar (i.e., hydrophobic) amino acids are mostly buried in the interior and hydrophilic (i.e., polar) amino acids are mostly on the surface.
  3. What are the basic components of an amino acid?
    • An alpha-carbon attached to:
    • - a Carboxyl group COOH
    • - and amino group -NH3
    • - R group - functional group
  4. Which amino acid is not optically active and why?
    Glycine because it is not chiral - hs 2 H's attached to the alpha carbon
  5. Of which configuration are all amino acids in mammalian proteins? D or L?
  6. Which amino acids are grouped as Hydrophobic (apolar) Aliphatic?
    • Glycine
    • Alanine
    • Valine
    • Leucine
    • Isoleucine
    • Methionine
    • Proline
    • (7 total)
  7. What structural properties are common among Hydrophobic aliphatic AA's and why are they important?
    • Apolar
    • R-groups comprised of saturated C backbones
    • Subtle differences in R-groups allows for tight packing within the protein interior
  8. What makes proline functionally different from other AA's?
    It is an imino AA - It has 2 N-C bonds whereas all others have an amino group