Friday, 26 March 2021

SPM Biology 3 Movement of Substances Across the Plasma Membrane Part 3 3 Types of Solution & the Effects of Different Concentrations of Solution on Cells

The direction of movement of substances across the plasma membrane in the cell depends on the concentration of the solution around it.

There are 3 types of solution:
  1. Hypertonic solution = solution with higher concentration of solutes than the cell. (lower water concentration)
  2. Hypotonic solution = solution with lower concentration of solutes than the cell. (higher water concentration)
  3. Isotonic solution = solution with equal solute concentration.
**osmosis happen when the water diffuse across the membrane from hypotonic solution to hypertonic solution***

Three types of solution
Three types of solution

















In hypertonic solution, red blood cells undergo crenation (water diffuse out from cell, cell shrivel and die). Plant cells undergo plasmolysis (plant cell loses water and shrivels, cell becomes flaccid, cause plant wilt). 

In hypotonic solution, red blood cells undergo hemolysis (the cell gain water and swell, finally burst because they no cell wall). Plant cells become turgid (vacuole gain water, expands and exerts pressure outwards on the cell wall).

In Isotonic solution, water diffuses into and out of the cell by osmosis at the same rate. The cells maintain their normal shape.


***terms hemolysis & crenation only for red blood cell.

Blood condition in different solutions
Blood condition in different solutions



STPM Biology Biological Molecules Part 16 Amino Acids - Properties of Protein

1. Protein is amphoteric.

  • Its structure has basic and acidic group.
  • Amino group, NH2 is basic; while carboxyl group, COOH is acidic.

Structure of amino acid
Structure of amino acid

2. Protein is an important buffer in biological systems.

  • The amphoteric nature of protein allows it to function as a buffer.
  • Amino groups of protein removes excess acids in the system.
  • Carboxyl groups neutralize the excess bases in the system.

Protein as buffer in biological system
Protein as buffer in biological system

3. The colloidal nature of proteins allow it to exist as individual molecules in solution.

  • Colloids are particles not soluble in water but remain suspended in the solution.
  • Colloidal particles are usually 1nm to 100nm in diameter.
  • Most globular proteins are soluble in water due to the small size of its molecule and existing polar groups such as -COOH.
  • Globular protein with larger molecules will from colloidal suspensions in water.
  • The colloidal nature of protein provides a larger surface are for biochemical reactions in cells.

Differences between solution, colloidal solution and suspensions
Differences between solution, colloidal solution and suspensions

4. Protein denaturation.

  • The change of structure and shape of the protein molecule due to the breaking down one or more bonds maintaining the structure of protein molecule is called protein denaturation.
  • It can be caused by acids, bases, heat, pH and ultraviolet light.

Protein denaturation
Protein denaturation

STPM Biology Biological Molecules Part 15 Amino Acids - Levels and Composition of Protein Structure

Levels of protein structure

1. Primary structure

  • Primary structure is structure showing the number and sequence of amino acids in its molecule.

Primary structure of insulin
Primary structure of insulin

2. Secondary structure

  • Secondary structure is the structure showing the coiling of polypeptides to become helix or the folding of polypeptide to become pleated-sheet.
  • Secondary structures are maintained and stabilized by hydrogen bonds.

Secondary structure of protein
Secondary structure of protein

3. Tertiary structure

  • Tertiary structure of protein is the structures showing how a single polypeptide chain (helix) is folded form a globular structure.
  • This structure is maintained by various bonds; among which are disulphide bonds, electrovalent bonds or hydrogen bonds.

Tertiary structure of protein
Tertiary structure of protein

4. Quaternary structure

  • Quaternary structures of protein is the structure showing how two or more polypeptide chains are bound together.
  • Examples of protein with quaternary structure are hemoglobin.


Quaternary structure of protein
Quaternary structure of protein


Four levels of protein structure
Four levels of protein structure













Composition and structures of protein

1. Proteins can be classified according to its composition or structure.

2. Based on composition, proteins can be grouped into:

  • simple protein
  • conjugated protein

3. Based on structure, proteins can be divided into:

  • Fibrous protein
  • globular protein


Simple protein

  • Proteins that contain amino acids only.
  • For examples: albumin, globulin, and histone.


Conjugated protein

  • Protein bounds to non-protein groups.
  • Non-protein groups which bound to proteins are known as prosthetic groups.
  • For example: hemoglobin.

Structure of hemoglobin
Structure of hemoglobin

Fibrous protein

(a) Fibrous protein consists of long and parallel polypeptide chains.

(b) The polypeptide chain in fibrous protein is usually coiled to form α-helix.

(c) Neighboring helical chains are usually cross-linked by hydrogen bonds, electrovalent bonds, or disulphide bonds.

(d) Fibrous protein are not soluble in water and are very strong.

(e) Examples of fibrous protein:

  • Collagen - in tendons, cartilages, bones and skin.
  • Myosin - structural protein in muscles.
  • Keratin - structural protein in hairs, nails, feathers and horns.
  • Elastin - found in ligaments.
  • Sclerotin - combines with chitin to form the exoskeleton of insects.

(f) Collagen is the most common protein in mammals.

  • This protein is a main structural component of connective tissues (cartilage, skin, tendons and ligaments).
  • The basic structure of collagen is a tropocollagen helix which consists of three polypeptide chains (helixes) twisted together.
  • The chains are stabilized by hydrogen bonds between the protein chains.

Collagen fiber
Collagen fiber


Globular protein

(a) In globular proteins, the polypeptides (helixes) are folded into globular structures.

(b) The globular structure is maintained and stabilized by hydrogen bonds, disulphide bonds and electrovalent bonds.

(c) Some globular proteins are soluble in water; some of them form suspension, and the rest are insoluble in water.

(d) Globular proteins are easily denatured. This is because the hydrogen bonds and disulphide bond in the molecule can easily be broken.

Denaturation of protein
Denaturation of protein


(e) Examples of globular protein:

  • Hemoglobin
  • Myoglobin
  • Hormones
  • Enzymes

Saturday, 20 March 2021

SPM Biology 3 Movement of Substances Across the Plasma Membrane Part 2 Passive Transport and Active Transport

The movement of substances across a plasma membrane occurs through Passive Transport and Active Transport


Passive Transport

Definition: The movement of substances across the plasma membrane from a region of high concentration to a region of low concentration (down the concentration gradient).


Characteristics:

1. Do not require energy.

2. Substances move across the plasma membrane through:

  • Phospholipid bilayer
  • Channel protein
  • Carrier protein

3. Three ways of passive transport:

  • Simple diffusion
  • Osmosis
  • Facilitated diffusion


Simple diffusion

1. Definition = the movement of molecules down the concentration gradient until equilibrium is reached.

2. The molecules are evenly distributed with uniform concentration.

3. The bigger the concentration gradient, the faster the rate of diffusion.

4. Soluble substances that can move through phospholipid bilayer as simple diffusion:

  • Small uncharged polar (water soluble) (e.g. oxygen, carbon dioxide, water)
  • Lipid soluble molecules (e.g. fatty acids, glycerol, vitamins A,D,E,K)

Simple diffusion
Simple diffusion


5. Examples of simple diffusion:

  • Gases exchange at alveolus and blood capillary
  • Gases exchange between body cell and blood capillary


Osmosis (the passive transport of WATER)

1. Definition = the diffusion of water molecules down their concentration gradient through a semi-permeable membrane (selectively permeable membrane).

2. Water molecules move from a region of higher water concentration to region of lower water concentration.

3. Examples: The absorption of water by root hairs of a plant.

Osmosis
Osmosis


Facilitated diffusion

1. Definition = the passive transport of substances across the phospholipid bilayer with the help of transport proteins (channel protein & carrier protein).

2. The rate of facilitated diffusion depends on:

  • The number of transport protein molecules in the membrane.
  • How fast they can move their specific solute.

3. Substances move through facilitated diffusion:

  • Channel protein: Small charged molecules (e.g. mineral ions).
  • Carrier protein: Uncharged polar molecules (molecules insoluble in fats) (e.g. glucose, amino acid).

4. Mechanism of carrier protein:

The solute moves to the specific binding site of the carrier protein.

The solute binds to the carrier protein at the binding site & triggers the carrier protein to change its shape.

Carrier protein changes its shape and moves the solute across the membrane.

 The carrier protein returns back to its original shape.


Facilitated diffusion
Facilitated diffusion


Active Transport

Definition: the movement of substances across the plasma membrane from a region of low concentration to a region of high concentration (against the concentration gradient).

  • Require Energy (ATP = Adenosine Triphosphate)
  • The transport protein use energy to change the shape of the protein & to pump or transport the substance across the membrane
  • Examples:
    • pumping of sodium ions (Na+) out of the cell
    • intake of mineral ions by the root hairs of a plant
Active Transport
Active Transport


Comparison between Passive Transport & Active Transport


Comparison between Passive Transport & Active Transport

Comparison between Passive Transport & Active Transport



Tuesday, 16 March 2021

STPM Biology Biological Molecules Part 14 Amino Acids - Structure and Functions of Protein

1. Two amino acids can linked together to form a dipeptide by a condensation reaction. In the dipeptide, the two amino acids are linked by a peptide bond.


Formation of peptide bond
Formation of peptide bond


2. Peptide bond can only be formed by condensation reaction between the carboxyl group of one and the amino group of another amino acid.
3. Further amino acids can be added on either end of the dipeptide to form a polypeptide. Proteins consists of one or more polypeptides.
Polypeptide chain
Polypeptide chain


Structure of protein
  1. A protein may contain up to 20 types of amino acids. 
  2. Amino acids in proteins are linked together by peptide bond.
  3. Proteins are polymers with a large relative molecular mass.
  4. Protein molecules may contain one or more polypeptide chains.
  5. A polypeptide chain has a carboxyl group, COOH at one end and an amino group, NH2 at the other end (refer to the diagram above).

Fibrous proteins
(a) In fibrous proteins, the polypeptide chains exist as long parallel helixes. Helixes are cross-linked by:
  • hydrogen bonds,
  • disulphide bonds, or
  • electrovalent bonds
(b) Examples of fibrous proteins are collagen, keratin and fibrin.


Globular proteins
(a) In globular protein, the polypeptide chains (helix) are tightly folded to form a globular molecules. 
(b) The globular structure is stabilized by cross links, such as disulphide bonds.
(c) Examples of globular proteins include enzymes, myoglobin, insulin and hemoglobin.
fibrous protein globular protein

Example of fibrous and globular protein
Example of fibrous and globular protein


Conjugated proteins
(a) A protein may conjugate with prosthetic groups such as lipid, polysaccharides, nucleic acid, metals and ions.
(b) Examples of conjugated proteins are lipoprotein, nucleoprotein, glycoprotein and hemoglobin.

Conjugated protein
Conjugated protein


Functions of protein

  1. Protein is an important structural construction material.
  2. Protein can also function as catalyst. Enzymes are proteins that catalyze biochemical reactions.
  3. Transport of oxygen and carbon dioxide. Transport proteins include hemoglobin, the carrier of oxygen in blood.
  4. Maintain pH of cytoplasm and blood.
  5. Proteins are stored in organisms for food and energy.
  6. Protein is also involved in the defense and protection of body against pathogens. Antibodies are proteins in the blood that destroys pathogens. Fibrinogen and prothrombin are involved in blood clotting. Mucus protects the epithelial layer of digestive organs.
  7. Functions as hormones. Insulin, prolactin, and thyroxin are all proteins.
  8. Protein is also involved in food digestion. Digestive enzymes are proteins.
  9. Proteins play an important role in movements and mobility. Actin and myosin are involved in muscle contraction and movements of an amoeba. 
  10. Protein such as thyroxine is important for growth.

Wednesday, 10 March 2021

STPM Biology Biological Molecules Part 13 Amino Acids

1. Protein is an organic compound consisting of carbon, hydrogen, oxygen, nitrogen and sometimes sulphur and phosphorus.

2. Protein is a natural polymer, the monomer of protein is amino acid.

3. The basic structure of amino acid:

Basic structure of amino acid
Basic structure of amino acid

4. Amino acid has a basic amino group, -NH2 and a acidic carboxyl group, -COOH and a side chain, R. There are 20 types of amino acids found in proteins. Different amino acids have different R chain.

Amino Acids
Three Letter Abbreviation
Alanine
Ala
Arginine
Arg
Asparagine
Asn
Aspartic acid
Asp
Cysteine
Cys
Glutamine
Gln
Glutamic acid
Glu
Glycine
Gly
Histidine
His
Isoleucine
Ile
Leucine
Leu
Lysine
Lys
Methionine
Met
Phenylalanine
Phe
Proline
Pro
Serine
Ser
Threonine
Thr
Tryptophan
Trp
Tyrosine
Tyr
Valine
Val


5. Amino acids can be classified into 4 major types based on the side chain (R).

  • Non-polar amino acids
  • Polar amino acids
  • Basic amino acids
  • Acidic amino acids


Non-polar amino acids

  • Non-polar amino acids are amino acids with a non-polar side chain
  • Examples: glycine, alanine, valine, leucine, methionine, isoleucine, phenylalanine, and tryptophan.
Non-polar amino acids
Non-polar amino acids


Polar amino acids

  • Polar amino acids are amino acids with a polar side group.
  • Examples: serine, threonine, asparagine, glutamine, tyrosine, and cysteine.
    Polar amino acids
    Polar amino acids


Basic amino acids

  • Basic amino acids have side chain which is an amino group, NH2, a base group. 
  • Examples: lysine, arginine, and histidine.

Basic amino acids
Basic amino acids


Acidic amino acids

  • Acidic amino acids have a side chain which is a carboxylic group, COOH.
  • Examples: aspartic acid and glutamic acid.
Acidic amino acids
Acidic amino acids

Sunday, 7 March 2021

SPM Biology 3 Movement of Substances Across the Plasma Membrane Part 1 Structure of Plasma Membrane

SPM Biology 3 Movement of Substances Across the Plasma Membrane Mind Map
SPM Biology 3 Movement of Substances Across the Plasma Membrane Mind Map


Need for Movement of Substances Across Membranes

  1. All the substances that are required by the cell (e.g. oxygen, water, mineral) have to be transported from the surroundings across the plasma membrane into the cell.
  2. All the waste products (e.g. carbon dioxide) have to pass through the plasma membrane to be excreted from the cell.


Structure of Plasma Membrane

Fluid Mosaic Model

A membrane is pictured as a mosaic because it has various protein molecules embedded in the phospholipid bilayer. Since the membrane is fluid, most of the individual protein and phospholipid molecules can drift laterally (slow movement away from the normal or original position) in the membrane.


The structure of plasma membrane is comprised of: 

  • Phospholipid bilayer
  • Various types of protein molecules

Fluid Mosaic Model
Fluid Mosaic Model

1. Phospholipid bilayer

  • Is an amphipathic molecules (has both hydrophilic region and hydrophobic region).
  • Polar head: hydrophilic (attracted to water).
  • Non-polar tail: hydrophobic (repelled by water).
  • Only allow some substances to cross the plasma membrane.
  • Small molecules & neutral molecules (e.g. water, oxygen, carbon dioxide, lipid-soluble molecules) can cross the membrane easily.

Phospholipid bilayer
Phospholipid bilayer


2. Protein molecules

  • Slightly bigger polar molecules (e.g. glucose, amino acids, charged ion) can cross the plasma membrane with the help of protein molecules called transport protein.
  • Transport proteins in the plasma membrane function as:- 
    • Carrier protein: a protein molecule that has a shape that fits the shape of a specific molecules so that it can only carry specific molecules across the membrane.
    • Channel protein: a pore made of protein that provides a passage for a particular solute to pass through.

****Big molecules (e.g. sucrose, protein, starch) cannot move across the membrane****


STPM Biology Biological Molecules Part 12 Lipid - Steroids

1. Steroid is very different in structure compared to lipid but is classified together with lipid because of their similar nature.

2. Steroid are abundant in animal tissues, but it is hardly found in plants.

3. All steroid molecules consist of four fused rings of carbon atoms. Different steroids have different functional groups attached to this ensemble of rings.


The typical steroid structure with 17 carbon atoms
The typical steroid structure with 17 carbon atoms


4. The most common steroid in the body is cholesterol. Many steroid hormones are produced from cholesterol.

5. Other examples are vitamin D2 (calcipherol), bile acids, sex hormones (testosterone, progesterone and oestrogen), and adrenaline.

Examples of steroids
Examples of steroids

6. Cholesterol is synthesized in the liver. The importance of cholesterol in health:

  • Cholesterol is important in the health of cell membrane. It is a major component in the cell membranes of animals.
  • Cholesterol is a precursor for synthesizing animal hormones such as progesterone, bile acids, oestrogen, and others. These hormones are important for the healthy functioning of organisms.
  • Used to synthesize vitamin D in the skin.
  • Excess cholesterol in the body can lead to arteriosclerosis, high blood pressure and heart attacks.

Arteriosclerosis
Arteriosclerosis

STPM Biology Biological Molecules Part 11 Lipid - Phospholipids

1. Phospholipid molecule is formed from the condensation of:

  • one glycerol molecule
  • two fatty acids molecules
  • one phosphoric acid molecule



Structure and symbol of a phospholipid molecule
Structure and symbol of a phospholipid molecule


2. Phospholipid is a major component of cell membrane and hence is distributed all over the body of an organism.


Structure of phospholipid molecule

  1. A phospholipid molecule consists of one glycerol molecule attached to two fatty acids chain and one phosphate group.
  2. Additional small molecules (usually polar) can be linked to the phosphate group to form a variety of different phospholipids.
  3. For instance, choline molecule attaches to the phosphate group of phospholipids to form lecithin. 
  4. Lecithin is the most common phospholipid in human bodies. The major phospholipids of cell membrane is lecithin. The fatty acids of lecithin is oleic acid (unsaturated) and stearic acid (saturated).

Structure of lecithin
Structure of lecithin


Physical properties of phospholipid

  1. The hydrophilic head of phospholipid molecules is soluble in water, while the hydrophobic tail is insoluble in water.
  2. In water, phospholipid molecules assemble into a droplet called micelle. On the surface of water, phospholipid molecules are assemble closely with hydrophilic heads dissolved in water and the tails jutting out of the surface.
    Assembly of phospholipid molecules on the water surface and in water
    Assembly of phospholipid molecules on the water surface and in water

  3. In cells, both the intracellular environment and the immediate external environment are water. This causes phospholipids to form bilayer. In this bilayer, the hydrophilic heads are on the outside (in contact with water); the tails of phospholipids point to the interior. This bilayer is the main structures in the formation of cell membrane.
    Cross section of a phospholipids bilayer
    Cross section of a phospholipids bilayer


Functions of phospholipid

  1. Phospholipids are the main structural components for cell membranes.
  2. Phospholipid such as lecithin is involved in the production of neurotransmitters such as acetylcholine in the neurons.
  3. Phospholipid molecules are usually involved in transporting fat in the body.

Monday, 1 March 2021

STPM Biology Biological Molecules Part 10 Lipid - Triglycerides

1. All fats and oils are triglycerides.

2. A triglyceride molecule is formed through condensation reaction between three fatty acids and one glycerol molecule.

3. Hydrolysis of a triglyceride molecule produces fatty acid molecules and glycerol molecule.

Condensation and hydrolysis reactions of triglyceride
Condensation and hydrolysis reactions of triglyceride


4. Each fatty acid molecule is linked to glycerol by an ester bond, -COO. 

Ester bond, -COO
Ester bond, -COO


5. Saturated fat is a fat that does not contain any C=C bond in its molecule. Most of the saturated fat exists as solids in room temperature.

6. Unsaturated fat is a fat that has one or more C=C bonds in its molecule.

  • Monounsaturated fat is fat with molecules that only has one double bond between its carbon atoms. For examples, sesame oil and groundnut oil.
  • Polyunsaturated fat is fat with molecules that have two or more doubles C=C bonds in its molecules. For examples, maize oil, linseed oil and cottonseed oil.
  • Polyunsaturated fat has a low boiling level, thus it exists as liquid in room temperature.

Saturated, monounsaturated and polyunsaturated fat molecules
Saturated, monounsaturated and polyunsaturated fat molecules


7. The consumption of food rich with saturated fat and cholesterol increases the risks of cardiovascular diseases. Saturated fat molecules and excess cholesterol deposit on the artery walls, thus narrowing it.


Physical properties of triglycerides

  • Not soluble in water, but soluble in organic solvents.
  • High relative molecular mass.
  • High ratio of hydrogen atoms to oxygen atoms in molecule.
  • Can be emulsified.
  • Fat usually exists as a solid while oil exists as liquid at room temperature.


Chemical properties of triglycerides

  • Triglycerides undergo hydrolysis to form fatty acids and glycerol.


Distribution of triglycerides in organisms

  • In adipose tissues underneath the skin.
  • Attached to the surface of visceral organs such as the heart, liver and digestive tracts.
  • In eggs.
  • In seeds (maize, peanuts and etc.).


Functions of triglycerides

  • Source of energy of organisms.
  • As food and energy stores for animals.
  • Major components of plasma membrane.
  • Heat insulation. Fat underneath the skin is a heat insulator for animals in cold region.
  • Water proofing. Oils and waxes on the outer surface of organisms waterproof the body.
  • Protection. Fats packed around visceral organs protect these organs.
  • Fat is a source of metabolic water for animals.
  • Fat is an important solvent for vitamins A,D,E,K and hormones in the body.
  • Saturated fat is the raw material for synthesizing cholesterol.
  • Buoyancy. Stored fats also aid buoyancy.