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Amino Acids, Proteins, and Enzymes

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Amino Acids, Proteins, and Enzymes Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation Primary Structure of Proteins ... – PowerPoint PPT presentation

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Title: Amino Acids, Proteins, and Enzymes


1
Amino Acids, Proteins, and Enzymes
  • Primary and Secondary Structure
  • Tertiary and Quaternary Structure
  • Protein Hydrolysis and Denaturation

2
Primary Structure of Proteins
  • The particular sequence of amino acids that is
    the backbone of a peptide chain or protein

Ala-Leu-Cys-Met
3
Secondary Structure Alpha Helix
  • Three-dimensional arrangement of amino acids with
    the polypeptide chain in a corkscrew shape
  • Held by H bonds between the H of N-H group and
    the O of CO of the fourth amino acid along the
    chain
  • Looks like a coiled telephone cord

4
Secondary Structure Beta Pleated Sheet
  • Polypeptide chains are arranged side by side
  • Hydrogen bonds form between chains
  • R groups of extend above and below the sheet
  • Typical of fibrous proteins such as silk

5
Secondary Structure Triple Helix
  • Three polypeptide chains woven together
  • Glycine, proline, hydroxy proline and
    hydroxylysine
  • H bonding between OH groups gives a strong
    structure
  • Typical of collagen, connective tissue, skin,
    tendons, and cartilage

6
Learning Check P1
  • Indicate the type of structure as
  • primary (2) alpha helix
  • beta pleated sheet (4) triple helix
  • Polypeptide chain held side by side by H bonds
  • Sequence of amino acids in a polypeptide chain
  • Corkscrew shape with H bonds between amino acids
  • Three peptide chains woven like a rope

7
Solution P1
  • Indicate the type of structure as
  • primary (2) alpha helix
  • beta pleated sheet (4) triple helix
  • 3 Polypeptide chain held side by side by H bonds
  • 1 Sequence of amino acids in a polypeptide chain
  • 2 Corkscrew shape with H bonds between amino
    acids
  • 4 Three peptide chains woven like a rope

8
Tertiary Structure
  • Specific overall shape of a protein
  • Cross links between R groups of amino acids in
    chain
  • disulfide SS
  • ionic COO H3N
  • H bonds CO HO
  • hydrophobic CH3 H3C

9
Learning Check P2
  • Select the type of tertiary interaction as
  • (1) disulfide (2) ionic
  • (3) H bonds (4) hydrophobic
  • A. Leucine and valine
  • B. Two cysteines
  • C. Aspartic acid and lysine
  • Serine and threonine

10
Solution P2
  • Select the type of tertiary interaction as
  • (1) disulfide (2) ionic
  • (3) H bonds (4) hydrophobic
  • A. 4 Leucine and valine
  • B. 1 Two cysteines
  • C. 2 Aspartic acid and lysine
  • 3 Serine and threonine

11
Globular and Fibrous Proteins
  • Globular proteins Fibrous proteins
  • spherical shape long, thin fibers
  • Insulin Hair
  • Hemoglobin Wool
  • Enzymes Skin
  • Antibodies Nails

12
Quaternary Structure
  • Proteins with two or more chains
  • Example is hemoglobin
  • Carries oxygen in blood
  • Four polypeptide chains
  • Each chain has a heme group to
  • bind oxygen

13
Learning Check P3
  • Identify the level of protein structure
  • 1. Primary 2. Secondary
  • Tertiary 4. Quaternary
  • Beta pleated sheet
  • Order of amino acids in a protein
  • A protein with two or more peptide chains
  • The shape of a globular protein
  • Disulfide bonds between R groups

14
Solution P3
  • Identify the level of protein structure
  • 1. Primary 2. Secondary
  • 3. Tertiary 4. Quaternary
  • 2 Beta pleated sheet
  • 1 Order of amino acids in a protein
  • 4 A protein with two or more peptide
  • chains
  • D. 3 The shape of a globular protein
  • E. 3 Disulfide bonds between R groups

15
Protein Hydrolysis
  • Break down of peptide bonds
  • Requires acid or base, water and heat
  • Gives smaller peptides and amino acids
  • Similar to digestion of proteins using enzymes
  • Occurs in cells to provide amino acids to
    synthesize other proteins and tissues

16
Hydrolysis of a Dipeptide
17
Denaturation
  • Disruption of secondary, tertiary and quaternary
    protein structure by
  • heat/organics
  • Break apart H bonds and disrupt hydrophobic
    attractions
  • acids/ bases
  • Break H bonds between polar R groups and
  • ionic bonds
  • heavy metal ions
  • React with S-S bonds to form solids
  • agitation
  • Stretches chains until bonds break

18
Applications of Denaturation
  • Hard boiling an egg
  • Wiping the skin with alcohol swab for injection
  • Cooking food to destroy E. coli.
  • Heat used to cauterize blood vessels
  • Autoclave sterilizes instruments
  • Milk is heated to make yogurt

19
Learning Check P4
  • What are the products of the complete hydrolysis
    of Ala-Ser-Val?

20
Solution P4
  • The products of the complete hydrolysis of
    Ala-Ser-Val are
  • alanine
  • serine
  • valine

21
Learning Check P5
  • Tannic acid is used to form a scab on a burn.
    An egg becomes hard boiled when placed in hot
    water. What is similar about these two events?

22
Solution P5
  • Acid and heat cause a denaturation of protein.
    They both break bonds in the secondary and
    tertiary structure of protein.
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