BIOCHEMISTRY

Marie Dale T. Peralis

Department of Physical Sciences
College of Science

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Proteins
The most abundant biological macromolecules, occurring in all cells and all parts
of cells

Made from amino acid

Functions

◦Structure –collagen, keratin

◦Catalysis –enzymes
◦Movement –myosin, actin
◦Transport –hemoglobin
◦Protection –antibodies

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Amino Acids
The building blocks of protein

The monomers of protein

Only 20 amino acids are usually found in proteins

Only amino acids with L-configurations are used as building blocks of proteins

Except for glycine, all amino acids exhibit chirality

Proline is a cyclic amino acid (imino acid)

Humans are incapable of synthesizing half of the 20 common amino acids, and these
essential amino acids must be provided in the diet.

Isoleucine and threonine have 2 chiral centers

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Structure of Amino Acid

• Amino group

• Carboxyl group

• R-group

General structure of an amino acid

(Proline, a cyclic amino acid, is the
exception.)

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20 Common Amino Acids
Amino Acids Can Be Classified by R Group
1. Nonpolar, aliphatic R
groups

The side chains of alanine, valine,

leucine, and isoleucine tend to
cluster together within proteins,
stabilizing protein structure by
means of hydrophobic interactions

The side chain of glycine makes no

real contribution to hydrophobic
interactions

The secondary amino (imino) group

of proline residues is held in a rigid
conformation that reduces the
structural flexibility of polypeptide
regions containing proline.

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2. Polar, uncharged R groups

The R groups of these amino acids

are more soluble in water, or more
hydrophilic, than those of the
nonpolar amino acids

The polarity of serine and threonine is

contributed by their hydroxyl groups;
that of cysteine by its sulfhydryl
group; and that of asparagine and
glutamine by their amide groups.

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3. Aromatic R Group

Tyrosine and tryptophan are significantly

more polar than phenylalanine,
because of the tyrosine hydroxyl group
and the nitrogen of the tryptophan
indole ring.

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4. Positively Charged (Basic) R
groups

The amino acids in which the R

groups have significant positive
charge at pH 7.0 are lysine, which has
a second primary amino group at the
ε position on its aliphatic chain;
arginine, which has a positively
charged guanidino group; and
histidine, which has an imidazole
group.

Histidine is the only common amino

acid having an ionizable side chain
with a pKa near neutrality.

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5. Negatively charged R groups

The two amino acids having R groups with a net

negative charge at pH 7.0 are aspartate and
glutamate, each of which has a second carboxyl
group.

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Amino Acids Can Be Classified by R Group
Nonpolar, aliphatic R groups Polar, uncharged R groups Aromatic R groups
1. Glycine Gly, G 1. Serine Ser, S 1. Phenylalanine Phe, F
2. Alanine Ala, A 2. Threonine Thr, T 2. Tyrosine Tyr, Y
3. Proline Pro, P 3. Cysteine Cys, C 3. Tryptophan Trp, W
4. Valine Val, V 4. Glutamine Gln Q
5. Leucine Leu, L 5. Asparagine Asn, N
6. Isoleucine Ile, I
7. Methionine Met, M Positively charged R groups Negatively charged R groups
1. Lysine Lys, K 1. Aspartate Asp, D
2. Histidine His, H 2. Glutamate Glu, E
3. Arginine Arg, R

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Amino acids
Nonpolar Amino Acids - hydrophobic

Polar - hydrophilic , contain polar groups that form H-bonds with water

Essential Amino Acids (cannot be made by the body)

WHT MILK FVR

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