Carbohydrate

MACROMOLECULES

Ms. Evi Elfrida | SLHS | Grade 11

 ❑ A carbohydrate (hydrate from carbon) is an organic compound with an
empirical formula of Cn(H2O)m
❑ Glucose : C6H12O6 or C6(H2O)6
❑ Structurically they are polyhydroxy aldehydes and ketones

Carbohydrate

❑ The word sacharide comes from Greek word sakharon/sakarum, meaning

“sugar”
❑ The names of the monosaccharides and disaccharides very often end in
the suffix –ose.

Ms. Evi Elfrida | SLHS | Grade 11

u The carbohydrates (saccharides) are divided into 4 chemical
group :
Structure

1. Monosaccharides (consists only a single type of sugar)

2. Disaccharides (made from 2 type of sugar)
3. Oligosaccharides
4. Polysacchrides

For example : blood sugar is the monosaccharide glucose, table sugar is the disaccharide
sucrose, and milk sugar is the disaccharide lactose

Ms. Evi Elfrida | SLHS | Grade 11

Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Identification of carbohydrate

Fehling reagent

Tollens reagent

Ms. Evi Elfrida | SLHS | Grade 11

Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
 PROTEIN

MACROMOLECULES

Ms. Evi Elfrida | SLHS | Grade 11

Proteins
 Most structurally & functionally diverse group of biomolecules
 Function:

 involved in almost everything

 Metabolism
 Support
 Transport
 Regulation
 Motion

Ms. Evi Elfrida | SLHS | Grade 11

Proteins
– Structure:
– monomer = amino acids
– 20 different amino acids
– 12 made by body
– 8 essential amino acids (must get from food)
– polymer = polypeptide
– protein can be one or more polypeptide chains folded &
bonded together ▪ Structure:
– large & complex molecules ◆ central carbon (α
carbon)
– complex 3-D shape ◆ amino group
◆ carboxyl group (acid)
◆ R group (side chain)
▪ variable group
chemical properties
of the amino acid
Rubisco hemoglobin
Ms. Evi Elfrida | SLHS | Grade 11
Nonpolar amino acids
▪ nonpolar & hydrophobic

Ms. Evi Elfrida | SLHS | Grade 11

Polar amino acids
▪ polar or charged & hydrophilic

Ms. Evi Elfrida | SLHS | Grade 11

 Amino acids
❑ Contain both an acidic functional group (COOH) and a basic one (-NH2), NH or N
❑ Thus reactions are highly pH dependent

pH dependent properties
❑ Zwitterionic
structures contain
both N-H+ and COO-.
❑ At low pH
protonate COO-.
❑ At higher pH :
lose H on N)

Ms. Evi Elfrida | SLHS | Grade 11

Leucine ionic forms
❑ Cation below pH 2.4
❑ Neutral between pH 2.4 and 9.6
❑ Anionic above pH 9.6

Leucine zwitterion

– pH>2.4
– pH < 9.6

Ms. Evi Elfrida | SLHS | Grade 11

 Peptides – Buildup/Breakdown
O O

H dehydration
H2N CH C OH + H N CH C OH
hydrolysis

CH3 H
alanine (ala) glycine (gly)

Peptide or amide linkage

O O
H
H2N CH C N CH C OH + H2O

CH3 H carboxylic acid

amine
end
end
alanylglycine (ala-gly) -a dipeptide Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
 Levels of Protein Structure
1. Primary structure - the sequence of amino acids in the
peptide chain and the location of the disulfide bridges.
2. Secondary structure - a description of the conformation/
shape of the backbone of the protein.
3. Tertiary structure - a description of the 3D structure of the
entire polypeptide.

If the protein has more than one chain it can have a

quaternary structure.
Ms. Evi Elfrida | SLHS | Grade 11
Ms. Evi Elfrida | SLHS | Grade 11
Primary (1°) structure
– Order of amino acids in chain
– amino acid sequence determined by gene (DNA)
– slight change in amino acid sequence can affect protein’s structure & it’s
function
– even just one amino acid change can make all the difference!

Sickle cell anemia

Ms. Evi Elfrida | SLHS | Grade 11

Ms. Evi Elfrida | SLHS | Grade 11
 Some Protein Sequences

Phe - Gln Oxytocin – contracts smooth muscle

(induces ‘labour’)
Tyr Asn
Cys Cys - Pro - Arg - Gly
S-S

Ile - Gln
Vasopressin - diuretic
Tyr Asn
Cys Cys - Pro - Leu - Gly
S-S Ms. Evi Elfrida | SLHS | Grade 11
 Val- Ile-Gly Insulin (21 + 30)
Glu
Gln
Cys Cys-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys-Asn
Cys-Thr-Ser-Ile

Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys-Gly
Leu Glu

His Arg

Gln- Asn-Val-Phe Gly

Thr-Lys-Pro-Thr-Tyr-Phe- Phe
Ms. Evi Elfrida | SLHS | Grade 11
 Secondary (2°) structure
▪ “Local folding”
▪ folding along short sections of polypeptide
▪ interaction between adjacent amino acids
▪ H bonds between
backbones (O:H)
▪ -helix (wool, hooves, claws, thorns, horns,
scales, horse hooves, tortoiseshell )
▪ -pleated sheet (silk and cobwebs)
▪ Fibrous proteins – only have secondary
structure
▪ Keratin
▪ Silk

Ms. Evi Elfrida | SLHS | Grade 11

Secondary Structure(20) - the -Helix
H-bonding -
intramolecular

Ms. Evi Elfrida | SLHS | Grade 11

Tertiary (3°) structure
– “Whole molecule folding” ❑ determined by interactions
between R groups
– created when the secondary
structure fold and form bonds to
stabilize the structure into a ❑ Hydrophobic interactions
❑ anchored by
unique shape disulfide bridges
– Arises from weaker attractive forces ❑ Ionic Bonds between R groups
(non polar dispersion forces) between ❑ Hydrogen bonds between
hydrophobic parts of the same chain that are backbones
widely separated in the primary structure, but ❑ Van der Waals Force
close in space ❑ Globular (spherical) protein :
– “intramolecular” keratin,silk,collagen
❑ Fibrous : enzyme
– Results in chain twisting and folding

Ms. Evi Elfrida | SLHS | Grade 11

Tertiary (3°)
structure

Ms. Evi Elfrida | SLHS | Grade 11

 Quaternary (4°) structure
– two or more tertiary folded peptide subunits bonded together to make a functional protein
– Hemoglobin – 4 polypeptides
– Collagen – 3 polypeptides

collagen =
skin & tendons
hemoglobin
Ms. Evi Elfrida | SLHS | Grade 11
Quaternary Structure of Proteins

Ms. Evi Elfrida | SLHS | Grade 11

 Protein structure (review)
R groups
hydrophobic interactions,
disulfide bridges, ionic bonds

3° multiple
polypeptides
hydrophobic
interactions
1°
aa sequence
peptide bonds
determined 2°
by DNA 4°
H bonds
Ms. Evi Elfrida | SLHS | Grade 11
Denaturation
any physical or chemical process that changes the protein structure and makes
it incapable of performing its normal function.

Examples:
· heating egg whites (irreversible)
· ‘permanent’ waving of hair (reversible)

1. Heat
2. Mechanical agitation
3. pH change
4. Inorganic salts
❑ disrupts H bonds, ionic bonds &
5. polar organic solvents disulfide bridges
❑ destroys functionality
6. Soaps and detergents

Ms. Evi Elfrida | SLHS | Grade 11

Protein in Human hair
❑ Keratin (fibrous protein) has the S containing amino acid cystine (14~18%) .
❑ S-S bonds (disulphide linkages) between cystine units give hair its strength by connecting the strands and
keeping them aligned
Animal hair protein composition
❑ Sheep’s wool: also the fibrous protein keratin, but with high glycine & tyrosine content

Ms. Evi Elfrida | SLHS | Grade 11

Ms. Evi Elfrida | SLHS | Grade 11
 LIPID

MACROMOLECULES
Lipids
Triglycerides – fats
and oils

Phospholipids

Waxes

– cholesterol

steroids
Ms. Evi Elfrida | SLHS | Grade 11
Triglycerides
– Fat molecules
– Structure = 3 fatty acids chains linked to glycerol
– Functions = long term energy storage and insulation for animals
– Can be saturated or unsaturated

3 fatty
Glycerol acids

Ms. Evi Elfrida | SLHS | Grade 11

Triglycerides – fats and oils Compare fats and oils:

• Solid / liquid at room temperature?

• Mainly plant/ animal in origin?
• Mainly saturated / unsaturated?
• High levels can contribute to cardiovascular disease?
• Examples?

Ms. Evi Elfrida | SLHS | Grade 11

Saturated fats
– All C bonded to H
– No C=C double bonds
– long, straight chain
– most animal fats and butter
– solid at room temperature
– contributes to
cardiovascular disease

Ms. Evi Elfrida | SLHS | Grade 11

Unsaturated fats
– At least one C=C double bond in
the fatty acids
– plant & fish fats
– vegetable oils
– liquid at room temperature

Ms. Evi Elfrida | SLHS | Grade 11

Saturated vs. unsaturated
saturated unsaturated

Ms. Evi Elfrida | SLHS | Grade 11

Triglyceride structure

Glycerol + 3 fatty acids ----------> triglyceride + 3water

Ms. Evi Elfrida | SLHS | Grade 11

Triglyceride structure
Glycerol + 3 fatty acids ----------> triglyceride + 3water
Fatty acids Stearic acid
in adipose tissue

Acid group
(carboxylic
acid group)

Oleic acid
in olive oil
Ms. Evi Elfrida | SLHS | Grade 11
 Triglyceride
One glycerol molecule attached to three fatty acid molecules
glycerol 3 fatty acids

Ester bond
1. Energy store
2. Thermal insulation
3. Protection-internal organs
4. Source of water when respired

Ms. Evi Elfrida | SLHS | Grade 11

Phospholipids
– Structure: 2 fatty acids chains + phosphate head
– Fatty acid chains = non-polar = hydrophobic “water fearing”
– Phosphate head = polar = hydrophillic “water loving”

– Function: make up cell membranes

(phospholipid bilayer)

Ms. Evi Elfrida | SLHS | Grade 11

Phospholipids
list the differences between a phospholipid and
triglyceride molecules:

Key words: hydrophobic, hydrophilic, polar, non-polar,

fatty acid ‘tails’, glycerol/phosphate ‘head’, ester bond
Ms. Evi Elfrida | SLHS | Grade 11
Steroids
– Structure: 4 fused Carbon rings
– examples:
– cholesterol – Function =control the
fluidity of the cell membrane
– hormones – Function = regulate
processes in the body (such as
pregnancy)
– vitamins (A, B, D) – Function = supports
metabolism and cell processes

Cholesterol Ms. Evi Elfrida | SLHS | Grade 11

Waxes

– Solid at room temp

– Insoluble in water
– Function:
– Protective covering for
animals and plants
– Examples:
– Beeswax
– Earwax
– Cuticle of leaf (keeps water in)

Ms. Evi Elfrida | SLHS | Grade 11