Lecture 3: Amino Acid Structures Flashcards

1
Q

Amino Acids and Protein Structure

A
  • 20 amino acids that have distinct side chains that contribute to protein structure and function
  • Non-covalent and covalent interactions between functional groups are important for holding protein together + interactions
  • Interaction of hydrophilic amino acids with water help solubilize some proteins
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2
Q

Amino acids

A
  • Amino acids made up of an amino group, carboxyl group, and R side chain
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3
Q

Chiral amino acids

A
  • Asymetric alpha carbon results in chirality
  • Chiral molecules are non-superimposable mirror images
  • L amino acids are found in plant and animal proteins
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4
Q

Non-covalent interactions

A
  • Hydrogen bonds can form between hydroxyl, carboxyl, thiol, and amino groups
  • Hydrogen bonds can form between amino acid side chains with protein structure
  • Can occur between aliphatic and hydrophobic side chains
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5
Q

Disulfide bonds

A
  • Disulfide bonds covalently cross-link two cysteines together
  • Disulfide bridges can be interchain or between different polypeptide chains
  • Linkages stabilize structures
  • Protein Disulfide Isomerase enzymes help catalyze oxidation reaction
  • Disulfide bonds can be broken by reducing agents in cytosol or in lab(B-mercaptoethanol)
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6
Q

Hydrophobic Amino Acids

A
  • Hydrophobic amino acids can be found in the interior of proteins, maximizing number of hydrophilic interactions with water
  • Hydrophobic amino acids can still be found on surface to allow for non-covalent interactions
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7
Q

Post Translational Modification

A
  • Additional or removal of functional groups can change structure of a protein and affect its function
  • Disulfide bond formation is example of PTM
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