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PROTEIN SHAPE 
PROTEIN STRUCTURE 
AND 
ENZYMES 
Proteins Part II
Types of proteins 
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
Functional protein consists of one 
or more polypeptides precisely 
twisted, folded and coiled. 
Denaturation is the 
process in which a 
protein unravels and 
loses its normal 
shape. 
Changes in pH 
and temperature
Bonds between amino acids (from monomers to 
polymers) 
chemical reaction: Dehydration 
Reaction
Structure of the Protein Any 
alteration 
in the 
structure 
or 
sequencin 
g changes 
the shape 
and 
function 
of the 
protein
Denaturing 
Alteration of the 
protein´s shape and 
thus functions 
through the use of 
Heat 
Acids 
Bases 
Salts 
Mechanical agitation
Denaturing a Protein
ENZYMES 
 Weaken chemical bonds. 
 Molecules absorb energy. 
 “start-up” energy is called 
Activation energy. 
 Heating up would cause 
unnecessary reactions to occur at 
once. 
 Catalysts (compounds that speed up 
reactions). 
 Lowers the energetic requirement.
Lock and 
key. 
Specific 
substrate 
for the 
enzyme.
 http://highered.mcgraw-hill. 
com/sites/0072495855/student_view0/chapter2/animation__how_enzymes_w 
ork.html
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
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
Quick Review 
Protein structure has 4 levels: 
a)Primary structure 
b)Secondary structure 
c)Tertiary structure 
d)Quaternary structure 
 Denaturation is the Alteration of the protein´s shape and thus 
functions through the use of 
Heat 
Acids 
Bases 
Salts 
Mechanical agitation

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Protein structure and shape, Denaturation and Enzymes

  • 1. PROTEIN SHAPE PROTEIN STRUCTURE AND ENZYMES Proteins Part II
  • 2. Types of proteins 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
  • 3. Functional protein consists of one or more polypeptides precisely twisted, folded and coiled. Denaturation is the process in which a protein unravels and loses its normal shape. Changes in pH and temperature
  • 4. Bonds between amino acids (from monomers to polymers) chemical reaction: Dehydration Reaction
  • 5. Structure of the Protein Any alteration in the structure or sequencin g changes the shape and function of the protein
  • 6. Denaturing Alteration of the protein´s shape and thus functions through the use of Heat Acids Bases Salts Mechanical agitation
  • 8. ENZYMES  Weaken chemical bonds.  Molecules absorb energy.  “start-up” energy is called Activation energy.  Heating up would cause unnecessary reactions to occur at once.  Catalysts (compounds that speed up reactions).  Lowers the energetic requirement.
  • 9. Lock and key. Specific substrate for the enzyme.
  • 11. 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
  • 12. 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
  • 13. Quick Review Protein structure has 4 levels: a)Primary structure b)Secondary structure c)Tertiary structure d)Quaternary structure  Denaturation is the Alteration of the protein´s shape and thus functions through the use of Heat Acids Bases Salts Mechanical agitation