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By: Emily, Kennedy

Uncommon Amino Acids, Amino Acids Forming Proteins & Primary Structure of a Protein ( 14.5-14.7) pg 309-315. By: Emily, Kennedy. 14.5 What Are Uncommon Amino Acids?. Derived from common amino acids Made from parent amino acids through post-transitional modification

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By: Emily, Kennedy

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  1. Uncommon Amino Acids, Amino Acids Forming Proteins & Primary Structure of a Protein(14.5-14.7) pg 309-315 By: Emily, Kennedy

  2. 14.5 What Are Uncommon Amino Acids? • Derived from common amino acids • Made from parent amino acids through post-transitional modification -Post- transitional modification: modification of amino acid after the protein is synthesized

  3. Examples of Uncommon Amino Acids • Connective tissue proteins, like collagen, contain hydroxyproline and hydroxylsine • Thyroxine is an extra iodine-containing aromatic group added as a side chain to tyrosine -released as a hormone through globylin

  4. 14.6 How Do Amino Acids Combine to Form Proteins? • Every amino acid contains a carboxyl and amino group (combined to make an amide) - Ex. O C – NH • Bonding in amino acids is a peptide bond • Product of 2 amino acids is called a dipeptide

  5. Constitutional isomers are made by switching the groups around but may change the structure & function of the protein • When more amino acids are added, tripeptides (3 amino acids linked), tetrapides (4 amino acids linked), and many other proteins are formed.

  6. Forms of chains • Peptides are the shortest chain • Polypeptides contain a chain of 30 to 50 amino acids linked together • Proteins are the longest chain

  7. Residues are separate amino acids in a chain represented by letters to stand for their names • C-terminal is an amino acid at the right end of a peptide with a free α-carboxylic group (-COOH) • N- terminal is an amino acid on the left end of a peptide with a free α– amino group (-NH3)

  8. Examples Of C & N terminals Alanylglycyllysine- AGK or Ala – Gly - Lys • C – terminal : Lysine • N – terminal : Alanine

  9. 14.7 What Are the Properties of Proteins? • Continous peptide bonds make the backbone of a protein. • Side chains: R groups branched off of backbone • Adjacent bonds can rotate around C – N & C – C

  10. Zwitterions • Proteins conatin zwitterions like amino acids • Glutamic & Aspartic are acidic • Lysine & Arginine are basic

  11. pH • Isoelectric point (I.P.) is the pH point of equal positive and negative charges • pH above I.P. is a negative charge • pH below the I.P. is a positive charge

  12. pH solubility • pH solubility depends on the forces on the surface • Causes to repel each other • Least soluble at I.P.

  13. Primary have a linear sequence of amino acids in a chain • Secondary have repeating patterns, pleated sheet, or coil • Tertiary are the overall formation of the chain • Quarternary contain more than one chain and show how they are related to one another

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