Amino acids, Biology

 

  • An amino acid is amphiprotic (have both acid and base)

             o    Some are polar, non polar, acidic or basic

  • List of amino acids (red are non-polar, yellow are polar, green are acidic, blue are basic, starred are essential)

 

  •  An amino acid is amphiprotic (have both acid and base)

             o    Some are polar, non polar, acidic or basic

  •  List of amino acids (red are non-polar, yellow are polar, green are acidic, blue are basic, starred are essential)

 
                o    Glycine (gly)
                o    Alanine (ala)
                o    Valine (val)*
                o    Leucine (leu)*                                                                                    
                o    Isoleucine (ile)*
                o    Methionine(met)*
                o    Phenylalanine(phe)*
                o    Tryptophan (trp)*
                o    Proline (pro)

               o    Serine (ser)

 

                                                                1512_properties of Amino Acids.png1568_Amino Acids.png

 

               o    Threonine(thr)*
               o    Cysteine (cys)
               o    Tyrosine (tyr)

               o    Asparagines (asn)
               o    Glutamine (gln)
               o    Glutamic Acid (glu)
               o    Aspartic Acid (asp)

              o    Lysine (lys)*
              o    Arginine (arg)

              o    Histidine (his)

Properties of Amino Acids

Peptide Bond - bond between the acid group of one amino acid and the amino group of another
Dipeptide - 2 amino acids joined by a

peptide bond

  • Coded for by DNA and created by the ribosomes
  • Proteins are long, flexible and able to form different links with themselves or other molecules
  • Have an amino(A)-terminus and a Carboxyl(C)-terminus

Protein Structure

  • A Protein's function depends on its shape which depends on its amino acids

 

  • Primary Structure
    • Long chain of amino acids linked by covalent peptide bonds à in specific order
  • Secondary Structure
    • Intermolecular forces (mostly H-bonds) cause the chain to coil into an α-helix or fold into a β-pleated sheet
  • Tertiary Structure
    • Chaperone proteins help a growing polypeptide fold into its tertiary structure
    • Supercoiling due to polarity, the shape of the amino acids (e.g. proline causes a kink), other components (e.g. iron) and disulfide bridges.
  • Quaternary Structure
    • Various polypeptides join together with intermolecular forces to form a protein

Denaturing of Proteins

  • Change in è Heat, pH, temperature, ionic concentration etc.
    • Can cause changes in the 3-D structure of the protein

                        Change can be permanent if the 1° structure is broken

                        Change can be reversed if only the 3° structure is broken

  • Use of denaturing proteins à Food preservation

 

 

 

Posted Date: 8/20/2012 4:24:44 PM | Location : United States







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