Biomolecules

- Organic compounds made by living things

- Biochemicals

Carbohydrates
- Most abundant compounds in nature - plants.
- Sweet and soluble in water.
- Contain either an aldehyde or keto group in the structure.
- They are polyhydroxy.
1. Source of chemical energy for cells in many living things — storage form of energy.
2. Part of the structural material of plants.

Classifications of Carbohydrates
1. Monosaccharides
- Basic units of carbohydrates cannot be hydrolysed into smaller units.
- simplest unit of carbohydrates.
- Provide immediate energy.
- Simple Sugar
a. Number of Carbon atoms
b. Functional group present
c. Ends with -ose.
Examples:
● Glucose
- Most abundant in nature
- Major source of energy for all organisms.

● Fructose
- Sweetest tasting of all sugars.
- Found in many fruits and in honey.
- Best source of energy for drained / tired people.

● Galactose
- Synthesized in humans.
- Used to differentiate between blood types.
- Brain Sugar

2. Disaccharides
 - Made by two monosaccharide units by glycosidic bond — Carbon-
Oxygen-Carbon bonding.
- Water would also be produced once bonded.
Examples:
● Lactose
- Galactose-Glucose
- Found in milk and dairy products.

● Maltose
- Glucose-Glucose
- Mainly produced by partial hydrolysis of starch.

3. Polysaccharides
- Made up of repeating units of monosaccharides held by glycosidic bonds.
- Ideal as storage and as structural components.
- Complex sugars
- Energy storage: starch (plants), glycogen (animal starch)
- Linear (Rigid and insoluble in water) or Branched (Water-soluble)
- Not sweet
- Glycans
Storage Polysaccharides (Homoglycans)
- Which are used as food storage or reserve energy.
a. Starch
- Carbohydrate reserve of plants.
- White, odorless, tasteless powder.
- Amylose (linear) - Amylopectin (branched)
- Amylum
b. Glycogen
- Carbohydrate reserve in animals — animal starch.
- High concentration- Liver, muscles, and brain.
- Glucose is the repeating unit.
c. Inulin
- Polymer of Fructose (ex.: fructosan)
- Found in Dahlia, bulbs, garlic, onion etc.

Structural Polysaccharides (Heteroglycans)

- Used to the creation of structural components of cells including cell
walls.
- Made up condensation of 2 or more types of monosaccharides
a. Cellulose
 - Most abundant organic substance in the plant kingdom.
- No animals have this.
b. Chitin
- Second most abundant organic substance.

Description of CHO structures

● Projection type (Fischer or Haworth)
● Number of C atoms in the structure
● Functional Group (Aldose or Ketose)
● D or L configure
● α (alpha) (opposite) or β (beta) (same side)
● Chirality — a molecule is chiral is to say that its mirror image (it
must have one) is not the same as itself.

Proteins
- Composed of 50 or more amino acids joined together by peptide bonds.
- Globular or Fibrous
- Life’s building blocks

Functions of Proteins
● Antibodies — protects you from infections.
● Repair
● Enzymes (or Catalysts) — help speed up the breakdown process.
● Hormones — Help control or regulate processes in the body.
● Source of Energy
● Transport of Substances — transports energy and nutrients through your
body.

Amino Acids
- Organic compounds that contain both amino and carboxylic acid functional
groups.
- 22 AA’s are used in the human body.
- Structure: Amino group (NH2), Carboxylic group (COOH), Hydrogen atom (H),
and the R-side chain.
- Building blocks of proteins.

Essential AA
- Cannot be produced by the human body.
 Histidine (His) (H) Methionine (Met) (M) Tryptophan (Trp) (W)

Isoleucine (Ile) (I) Phenylalanine (Phe) (F) Valine (Val) (V)

Leucine (Leu) (L) Threonine (Thr) (T) Lysine (Lys) (K)

Conditionally Non-Essential AA
- pqCan be produced by the human body in different conditions.
Arginine (Arg) (R) Glycine (Gly) (G) Serine (Ser) (S)

Asparagine (Asn) (N) Proline (Pro) (P)

Glutamine(Gln) (Q) Tyrosine (Tyr) (Y)

Non-Essential AA
- Can be produced by the human body.
Alanine (Ala) (A) Cysteine (Cys) (C)

Aspartate (Asp) (D) Glutamate (Glu) (E)

 Classification of Protein Structure
1. Monomeric
- Proteins composed of a single polypeptide chain.

2. Multimeric
- Consisting of multiple protein molecules as their monomeric units,
connected through covalent or non-covalent bonds.

Levels of Protein Structure

1. Primary Structure
- The exact ordering of amino acids forming their chains.
- Sequence of amino acids in the peptide chain.

2. Secondary Structure
 - Local folded structures that form within a polypeptide due to interactions
between atoms.
a. α – Helix
- Hydrogen bonds between every fourth amino acid.
- A coiled structure, with 3.6 amino acids per turn of the helix.
b. β – Pleated Sheet
- Hydrogen bonds between two side-by-side chains, or a single chain
that is folded back on itself.
- Organized to form elaborately organized structures, such as
sheets, barrels, and other arrangements.

3. Tertiary Structure
- Three-dimensional structure that results in attractive forces between
amino acid side chains that are not near each other.
- Bonds: Disulfide bonds (Cysteine, because it has sulfur), Electrostatic
interactions, Hydrogen bond, Hydrophobic interactions
- Hydrophilic (Polar) or Hydrophobic (Nonpolar, water hater)

4. Quaternary Structure
- Three-dimensional shape of a protein consisting two or more independent
peptide chains that came from non covalent interactions between R
chains.
- Bonds: Electrostatic interactions, Hydrogen bonds, Hydrophobic
interactions

Protein Denaturation
- Any changes in the three-dimensional structure of a protein that renders it
incapable of performing its assigned function.
- Involves the breaking of many of the bonds within a protein molecule that are
responsible for the highly ordered structure.
- Factors: Changing solvent, changing Ph, adding ionic substances, raising the
temperatures, violent agitation

Shapes of Protein
1. Fibrous Protein
- Helps to maintain cell shape by providing a scaffolding.
- Amino acid sequence is repetitive in nature
- Hydrophobic
- Examples: Keratin, collagen, elastin, fibrin
 2. Globular Protein
- Carry out a specific biological function in the body.
- Amino acid sequence is irregular
- Water-soluble
- Examples: Hemoglobin, myoglobin, insulin, enzymes

3. Membrane Protein
- Proteins being associated or attached to the membrane of a cell or an
organelle inside the cell.
- Integral (temporally associated with the lipid bilayer) and Peripheral (permanently
embedded).

Protein Synthesis
- The process in which cells make proteins
● Ribosomes — responsible for synthesizing proteins by translating the genetic
code transcribed in mRNA into an amino acid sequence
● Golgi Body/Apparatus — The transport, sorting and modification of both protein
and lipid.

Two Phases of Protein Synthesis

1. Transcription
- A process by which DNA directs the synthesis of mRNA molecules.
- The transfer of genetic instructions in DNA to mRNA in the nucleus.

2. Translation
- A process in which mRNA is deciphered to synthesize a protein molecule.
- It is the process in which the genetic code in mRNA is read to make a
protein.

Types of RNA Molecules

1. Heterogeneous Nuclear RNA (hnRNA)
- Formed directly by DNA transcription.
- Post-transcription processing converts the hnRNAto messenger RNA
(mRNA). (it will become mRNA)

2. Messenger RNA (mRNA)

 - Carries instructions for protein synthesis (genetic information) from DNA.

3. Small nuclear RNA (snRNA)

- Facilitates the conversion of hnRNAto mRNA. Contains from 100 to 200
nucleotides.
- Processing of pre-messenger RNA (hnRNA) in the nucleus.

4. Ribosomal RNA (rRNA)

- Combines with specific proteins to form ribosomes — the physical site for
protein synthesis.
- Exported to the cytoplasm to help translate the information in messenger
RNA (mRNA) into protein.

5. Transfer RNA (tRNA)

- Delivers amino acids to the sites for protein synthesis tRNAs are the
smallest (75–90 nucleotide units).

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