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© 2010 Pearson Education, Inc.
Chapter 6: Proteins and
Amino Acids
© 2010 Pearson Education, Inc.
What Are Proteins?
 Large molecules
 Made up of chains of amino acids
 Are found in every cell in the body
 Are involved in most of the body’s functions and life
processes
 The sequence of amino acids is determined by DNA
© 2010 Pearson Education, Inc.
Structure of Proteins
 Made up of chains of amino acids; classified by number of
amino acids in a chain
• Peptides: fewer than 50 amino acids
- Dipeptides: 2 amino acids
- Tripeptides: 3 amino acids
- Polypeptides: more than 10 amino acids
• Proteins: more than 50 amino acids
- Typically 100 to 10,000 amino acids linked together
 Chains are synthesizes based on specific bodily DNA
 Amino acids are composed of carbon, hydrogen, oxygen,
and nitrogen
Structural Differences Between Carbohydrates,
Lipids, and Proteins
Figure 6.1
The Anatomy of an Amino Acid
Figure 6.2b
© 2010 Pearson Education, Inc.
Peptide Bonds Link Amino Acids
 Form when the acid group (COOH) of one amino acid joins
with the amine group (NH2) of a second amino acid
 Formed through condensation
 Broken through hydrolysis
Condensation and Hydrolytic Reactions
Figure 6.3
© 2010 Pearson Education, Inc.
Essential, Nonessential, and Conditional
 Essential – must be consumed in the diet
 Nonessential – can be synthesized in the body
 Conditionally essential – cannot be synthesized due to
illness or lack of necessary precursors
• Premature infants lack sufficient enzymes needed to
create arginine
© 2010 Pearson Education, Inc.
Structure of the Protein
 Four levels of structure
• Primary structure
• Secondary structure
• Tertiary structure
• Quaternary structure
Any alteration in the structure or sequencing changes
the shape and function of the protein
© 2010 Pearson Education, Inc.
Denaturing
 Alteration of the protein’s shape and thus functions
through the use of
• Heat
• Acids
• Bases
• Salts
• Mechanical agitation
 Primary structure is unchanged by denaturing
Denaturing a Protein
Figure 6.5
© 2010 Pearson Education, Inc.
Quick Review
 Proteins are chains of combination of amino acids
 Amino acids contain carbon, hydrogen, oxygen, nitrogen,
and sometimes sulfur
 Unique amino acids consist of a central carbon with a
carboxyl group, a hydrogen, a nitrogen-containing amine
group, and a unique side chain
 There are 20 side chains and 20 unique amino acids
• 9 essential amino acids
• 11 nonessential amino acids
- At time these become conditionally essential
 Amino acids link together with peptide bonds by
condensation and break apart by hydrolysis
© 2010 Pearson Education, Inc.
Quick Review
 Attractions and interactions between the side chains cause
the proteins to fold into precise three-dimensional shapes
 Protein shape determines its function
 Proteins are denatured and their shapes changed by
• Heat
• Acids
• Bases
• Salts
• Mechanical agitation

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Proteins.ppt

  • 1. © 2010 Pearson Education, Inc. Chapter 6: Proteins and Amino Acids
  • 2. © 2010 Pearson Education, Inc. What Are Proteins?  Large molecules  Made up of chains of amino acids  Are found in every cell in the body  Are involved in most of the body’s functions and life processes  The sequence of amino acids is determined by DNA
  • 3. © 2010 Pearson Education, Inc. Structure of Proteins  Made up of chains of amino acids; classified by number of amino acids in a chain • Peptides: fewer than 50 amino acids - Dipeptides: 2 amino acids - Tripeptides: 3 amino acids - Polypeptides: more than 10 amino acids • Proteins: more than 50 amino acids - Typically 100 to 10,000 amino acids linked together  Chains are synthesizes based on specific bodily DNA  Amino acids are composed of carbon, hydrogen, oxygen, and nitrogen
  • 4. Structural Differences Between Carbohydrates, Lipids, and Proteins Figure 6.1
  • 5. The Anatomy of an Amino Acid Figure 6.2b
  • 6. © 2010 Pearson Education, Inc. Peptide Bonds Link Amino Acids  Form when the acid group (COOH) of one amino acid joins with the amine group (NH2) of a second amino acid  Formed through condensation  Broken through hydrolysis
  • 7. Condensation and Hydrolytic Reactions Figure 6.3
  • 8. © 2010 Pearson Education, Inc. Essential, Nonessential, and Conditional  Essential – must be consumed in the diet  Nonessential – can be synthesized in the body  Conditionally essential – cannot be synthesized due to illness or lack of necessary precursors • Premature infants lack sufficient enzymes needed to create arginine
  • 9.
  • 10. © 2010 Pearson Education, Inc. Structure of the Protein  Four levels of structure • Primary structure • Secondary structure • Tertiary structure • Quaternary structure Any alteration in the structure or sequencing changes the shape and function of the protein
  • 11. © 2010 Pearson Education, Inc. Denaturing  Alteration of the protein’s shape and thus functions through the use of • Heat • Acids • Bases • Salts • Mechanical agitation  Primary structure is unchanged by denaturing
  • 13. © 2010 Pearson Education, Inc. Quick Review  Proteins are chains of combination of amino acids  Amino acids contain carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur  Unique amino acids consist of a central carbon with a carboxyl group, a hydrogen, a nitrogen-containing amine group, and a unique side chain  There are 20 side chains and 20 unique amino acids • 9 essential amino acids • 11 nonessential amino acids - At time these become conditionally essential  Amino acids link together with peptide bonds by condensation and break apart by hydrolysis
  • 14. © 2010 Pearson Education, Inc. Quick Review  Attractions and interactions between the side chains cause the proteins to fold into precise three-dimensional shapes  Protein shape determines its function  Proteins are denatured and their shapes changed by • Heat • Acids • Bases • Salts • Mechanical agitation