PROTEINS

GENE PRODUCTS
 OUTLINE

STRUCTURE, CHIRALITY, CLASSIFICATION

AMINO ACIDS PROPERTIES

PEPTIDE BOND

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 OUTLINE

LEVELS OF PROTEIN STRUCTURE

DENATURATION PROTEINS

PROTEIN CLASSIFICATION

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 AMINO ACIDS
MONOMERS OF PROTEINS

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 AMINO ACIDS

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 AMINO ACIDS

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 AMINO ACIDS

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 Amino acid Essential / Non- Polarity
essential R group

Glycine, Gly, G NE Nonpolar

Alanine, Ala, A NE Nonpolar Aliphatic
Valine, Val, V E Nonpolar hydrocarbon
Leucine, Leu, L E Nonpolar
Isoleucine, Ile, I E Nonpolar
Serine, Ser, S NE Polar, neutral Hydroxyl group
Threonine, Thr, T E Polar, neutral Hydroxyl group
Tyrosine, Tyr, Y NE Polar, neutral Hydroxyl / Aromatic
group
Cysteine, Cys, C NE Polar, neutral
Sulfur group
Methionine, Met, M E Polar, neutral
Lysine, Lys, K E Polar, (+)
Basic amino acids
Arginine, Arg, R E Polar, (+)
Histidine, His, H E Polar, (+) Basic / Aromatic
group
Aspartic acid, Asp, D NE Polar, (-)
Acidic amino acids
Glutamic acid, Glu, E NE Polar, (-)
Asparagine, Asn, N NE Polar, neutral
Amide group
Glutamine, Gln, Q NE Polar, neutral
Proline, Pro, P NE Polar, neutral Imino acid 8
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Phenylalanine, Phe, F E Polar, neutral
Aromatic group
Tryptophan, Trp, W E Polar, neutral
 AMINO ACID: EXAMPLE

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 AMINO ACID: ACID-BASE PROPERTIES

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 AMINO ACID: ACID-BASE PROPERTIES

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 AMINO ACID: ACID-BASE PROPERTIES

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 AMINO ACID: ACID-BASE PROPERTIES

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 AMINO ACID: ELECTROPHORESIS

14

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 PROTEINS
FUNCTIONAL POLYPEPTIDES

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 LEVELS OF PROTEIN STRUCTURE

a. Primary: amino b. Secondary:

acids covalently arrangement in
linked together; space of atoms in
sequence the peptide
structure backbone.

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 LEVELS OF PROTEIN STRUCTURE

Alpha-helix (α- helix):

twisted in an equal
amount of carbons (3.6
L-aminoacyl residues);
R-groups face
outward; right-handed;
stability is due to the H-
bond between the O
of carbonyl and H of Source:
https://masteringcollegebioc
nitrogen at the 4th hemistry.wordpress.com/cat
egory/proteins/secondary-
residue. structure/

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 LEVELS OF PROTEIN STRUCTURE

Beta-sheets/Beta
pleated sheets (β-
sheets): R-groups of
adjacent residues
point in the opposite
direction; H-bond
between strands; can
be parallel or Source:

anti-parallel; usual core https://masteringcollegebioc

hemistry.wordpress.com/cat
of globular proteins. egory/proteins/secondary-
structure/

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 LEVELS OF PROTEIN STRUCTURE

Tertiary:
3D structure of the
peptide; domains
are present.
Source:
https://www.rcsb.org
/structure/1TES

1TES: Myoglobin

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 LEVELS OF PROTEIN STRUCTURE

Quaternary:
oligomeric protein;
spatial relationships
between subunits.
Source:
https://www.rcsb.org
/structure/1SI4

1SI4: Hemoglobin

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 PROTEIN DENATURATION

-unfolding and disorganization of protein’s secondary and

tertiary structures, without the hydrolysis of peptide bonds;
may be reversible; if irreversible, the protein can be
precipitated.

Source:
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Fib.bioninja.com.au%2Fstan
dard-level%2Ftopic-2-
molecular-biology%2F24-
proteins%2Fdenaturation.ht
ml&psig=AOvVaw0XRAKM7
XE6p4Fa3U8WhXke&ust=16
17011540470000&source=im
ages&cd=vfe&ved=0CAIQj
RxqFwoTCNCW7Mfb0u8CF
QAAAAAdAAAAABAD

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 PROTEIN CLASSIFICATION: BASED ON SHAPE

Fibrous Proteins: secondary structure

Collagen: most abundant protein in the human body; composed of 3 polypeptides forming
a triple helix.
Examples:
1. Fibril-forming collagen: type I, II, and III
2. Network-forming collagen: IV & VII
3. Fibril-associated collagen: type IX and XII
Structure:
• Amino acid sequence: polytripeptide
o Proline: facilitates the helical formation of each α chain.
o Glycine: found in every 3rd position; -Gly-X-Y-, where X is proline and Y is often
hydroxyproline or hydroxylysine.
• Glycosylation: hydroxylysine residues + glucose or galactose

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 PROTEIN CLASSIFICATION: BASED ON SHAPE

Globular Proteins (Heme proteins): tertiary and quaternary

Heme: a tightly bound prosthetic group
Example:
Hemoglobin: has a heme complex made of protoporphyrin IX and ferrous ion
HbA: a major hemoglobin in adults; composed of 4 polypeptide chains: 2 α chains
and 2 β chains held by non-covalent interactions forming 2 identical dimers αβ1
and αβ2 held hydrophobic interactions.
• T (taut/tense) form: deoxy form; low-oxygen affinity
• R (relaxed) form: oxygenated; high-oxygen affinity

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 PROTEIN CLASSIFICATION: BASED ON FUNCTION

1. Storage: provide nourishment

2. Movement: muscle contraction
3. Structural: maintain cell shape
4. Transport: distribution of nutrients
5. Defense: protection from pathogens
6. Signaling: coordinate bodily activities
7. Receptor: receiving instructions
8. Enzymes: catalytic action

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THANK
YOU
QUESTIONS/CLARIFICATIONS?