Protein

Group 1
Dita Luthfia
Nofita Lasari
Ranny Apriani Hapsari
Shohibatul Aslamiah
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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

2010 Pearson Education, Inc.

The Anatomy of an Amino Acid

Figure 6.2b

Condensation and Hydrolytic Reactions

Figure 6.3

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.

Hierarchical nature of protein structure

Primary structure (Amino acid sequence)

Secondary structure -helix, -sheet

Tertiary structure Three-dimensional structure

formed by assembly of secondary structures

Quaternary structure Structure formed by more than

one polypeptide chains

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Protein Folding

2010 Pearson Education, Inc.

2 regular folding patterns

have been identified
formed between the bonds
of the peptide backbone
-helix protein turns like
a spiral fibrous proteins
(hair, nails, horns)
-sheet protein folds back
on itself as in a ribbon
globular protein

Denaturing a Protein

Figure 6.5

Different Subunit Proteins

Hemoglobin
2 globin
subunits
2 globin
subunits

Antibody Family
A family of proteins that can be created to bind to
almost any molecule
Antibodies (immunoglobulins) are made in response to
a foreign molecule ie. bacteria, virus, pollen
called the antigen
Bind together tightly and therefore inactivates the
antigen or marks it for destruction

Antibodies
Y-shaped molecules with 2
binding sites at the upper ends
of the Y
The loops of polypeptides on the
end of the binding site are what
imparts the recognition of the
antigen
Changes in the sequence of the
loops make the antibody
recognize different antigens specificity

Antibodies

Protein Digestion: Part 1

Figure 6.6

Protein Digestion: Part 2

Figure 6.6

Protein Digestion: Part 3

Figure 6.6

Protein Digestion: Part 4

Figure 6.6

Amino Acid Absorption

Amino acids are absorbed in the small intestine

Amino acids are transported to the liver from the intestines
via the portal vein
In the liver, amino acids are
Used to synthesize new proteins
Converted to energy, glucose, or fat
Released to the bloodstream and transported to cells
throughout the body
Occasionally proteins are absorbed intact

2010 Pearson Education, Inc.

Protein Synthesis

Figure 6.8

Metabolic Fate of Amino Acids

Figure 6.7

Eating Too Much Protein

Risk of heart disease

Risk of kidney stones
Risk of calcium loss from bones
Risk of colon cancer
Displacement of other nutrient-rich, disease preventing
foods

2010 Pearson Education, Inc.

Eating Too Little Protein

Protein-energy malnutrition (PEM)
Protein is used for energy rather than its other functions in the
body
Other important nutrients are in short supply
More prevalent in infants and children
- 17,000 children die each day as a result
Without adequate protein
Cells lining the GI tract are not sufficiently replaced as they
slough off
Digestive function is inhibited
Absorption of food is reduced
Intestinal bacteria gets into the blood and causes septicemia
Immune system is compromised due to malnutrition and cannot
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Education,
Inc.
fight
infection

Enzymes

22

What Are Enzymes?

Enzym, from Greek

en-, in; zm,
leaven, yeast.
Most enzymes are
Proteins (tertiary
and quaternary
structures)

23

Enzymes

Are specific for

what they will
catalyze
Are Reusable
End in ase
-Sucrase
-Lactase
-Maltase

24

Making reactions go faster

Increasing the temperature make molecules
move faster
Biological systems are very sensitive to
temperature changes.
Enzymes can increase the rate of reactions
without increasing the temperature.
They do this by lowering the activation
energy.

2007 Paul Billiet ODWS

Enzymes

26

Enzyme-Substrate Complex
The substance
(reactant) an
enzyme acts on
is the substrate
Substrate

Joins

Enzyme

27

Active Site
A restricted region of an enzyme
molecule which binds to the substrate.
Active
Site
Substrate

Enzyme

28

Enzymes
Lock and Key Analogy: lock = enzyme, key
= substrate.

Induced Fit

A change in the
shape of an
enzymes active
site
Induced by the
substrate

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PROPERTIES OF ENZYME
1. As Catalyst / Biokatalisator
2. Specific
3. Its activity are affected by several
factors
4. Did not enter reacts
5. Worked two-way
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What Affects Enzyme Activity?

Three factors:
1. Environmental Conditions
2. Cofactors and Coenzymes
3. Enzyme Inhibitors

32

Two examples of Enzyme

Inhibitors
a. Competitive inhibitors: are

chemicals that resemble an

enzymes normal substrate and
compete with it for the active
site.
Substrate

Competitive inhibitor

Enzyme

33

Inhibitors
b.

Noncompetitive inhibitors:
Inhibitors that do not enter the
active site, but bind to another part
of the enzyme causing the enzyme to
change its shape, which in turn
alters the active site.

Substrate
active site
altered

Enzyme

Noncompetitive
Inhibitor

34

c. Uncompetitive inhibitors:
In uncompetitive inhibition, an enzyme inhibitor
is thought to bind to the E+S structure, or both
the enzyme and the substrate together. When
this happens, the product is unable to form,
thus also inhibiting the product.

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