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

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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 -Post- transitional modification: modification of amino acid after the protein is synthesized

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

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

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.

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

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)

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

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

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

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

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

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