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Lecture 2

BIOL107 Lecture Notes - Lecture 2: Proteinogenic Amino Acid, Leucine, Lysine


Department
Biology (Biological Sciences)
Course Code
BIOL107
Professor
Cirelli,Damián
Lecture
2

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January 11, 2109
Complex lipid- saccharide molecules
Lipoplysaccharides
Structural component of cell walls of some bacteria.
Proteins
a. Amino acids (monomers)
b. Polypeptides (polymer of amino acids)
c. Proteins (folded polypeptides)
Amino Acids
Contain an amino acid group and a carboxyl group
There are 20 proteinogenic amino acids with two extra that can be added.
There are other amino acids that are not incorporated in protein but with
important functions like GABA, a neurotransmitter.
Amino acids are classified into 4 groups according to their side chains.
The four groups include non-polar( hydrophobic) side chains called Leucine,
uncharged polar called Serine, negatively charged (acidic) called Aspartic acid,
positively charged (basic) called Lysine.
Bond, “The Peptide” Bond
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Two amino acids join to form dipeptide.
Just like carbohydrate polymers, amino acid polymerization requires
dehydration reaction.
Polypeptides
Sufficiently-long chains of peptides are polypeptides
The “average” human proteins contains 450 residues
It weighs 50,000 Daltons or 50kDa
Protein
When one or more polypeptide chains are folded in specific way, they become a
protein.
Polypeptide chains fold into the shape that takes the lowest possible energy.
Primary Structure (sequence)
Is simply the sequence, the order of amino acids.
Secondary Structure (first fold)
the first-order fold that forms
dominated by hydrogen bonds (H-bonds)
a helix is most common (a helix is the biggest sequence)
B pleated sheets can form also
And also:
Loops (hairpin)
Coils (undefined)
Is when the amino acids start interacting.
Tertiary Structure (folding of the folding)
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