Long chain molecule made up of a repeated pattern of monomers
What is the bond formed between 2 amino acids
Dipeptide
Where does the peptide bond specifically happen
It happens between the carboxyl group of oneamino acid and the amino groups
What are the different protein structure
Primary Secondary Tertiary and Quaternary
Primary structure
The sequence of the amino acid
Secondary Structure
The protein structure is folded into an alpha helix or beta pleated helix stabilised by the hydrogen bonds
Tertiary structure
Folds into a 3D shape of the proteins entire polypeptide chain which is stabilised by a various of bonds
What is Protein?
Protein is an essential biological molecule that plays a crucial role in various cellular processes, including enzyme activity, structure, hormones,immune response, transportation, and regulation.
What is the basic unit for Protein
Amino Acid
How are Disaccharides formed
When two monosaccharides unit joined by glycosidic bond
Example of a monosaccharide
Glucose Fructose and Galactose
Example of disaccharides
SucroseLactoseMaltose
Monosaccharides
Simplest form of Carbohydrates
Polysaccharides
Complex Carbohydrates composed of many monosaccharides units joined by glycosidic bonnds
Use of lipids
Important constituent of cell membranes
Cell signaling
Storing energy for the future
Can be used fuel
Triglycerides
A type of fatty molecules that play a crucial role in energy storage and metabolism. They are formed by a condensation molecule of glycerol and three molecules of fatty acids
The structure of a phospholipid
They contain 2 fatty acids, tails attached to a molecule of glycerol and a phosphate group
What is the head and tail of the phospholipid structure
The head is Hyrdrophillic (attracts water)
The tail is Hydrophobic (repels water)
Ester Bond
A type of chemical bond formed between a hydroxyl group and a carboxyl group through a condensation reaction
Hydrolysis
A chemical reaction in which a molecule is brokendown into two or more smaller moleculesusing water, often used to break down ester bonds
Glycosidic Bond
A type of covalent bond formed between a sugar molecule and a hydroxylgroup of another molecule through a condensation reaction
What are enzymes?
Biologicalcatalysts that speed up chemical reactions in living organisms without being consumed.
What factors affect enzyme activity?
Temperature
Optimal range; too high causes denaturation
Too low reduces activity
pH
Each enzyme has an optimal pH
Substrate concentration
Higher concentration increases reaction rate
Enzyme concentration
More enzyme typically means faster reactions
Inhibitors
Competitive and non-competitive
Cofactors and coenzymes
Some enzymes require these to function
What happens to enzyme activity at high temperatures?
The enzyme denatures, losing its shape and function.
Plasma Membrane
Fill in the blanks
A) Glycerol
B) Fatty Acids
C) Chloestrol
D) Intergal Protein
E) Channel Protein
F) Phospholipid Bilayer
G) Glycoprotein
Phospholipid in a plasma membrane
Arranges themselves into a bilayer with the hydrophilic head to the aqueous water environment outside and the hydrophobic tails tucked away
What does the cholesterol do
Stabilises the membrane and makes it better at controlling what it is that can pass through
Regulates the fluidity and permeability of the membrane
Intergal Protein
Transports large molecules across the membrane
Peripheral Protein
Involved in communication and some transport
Glycoproteins
Involved in cell recognition
Relationship between the size and surface area: volume ratio
Each time a cell increases in size the surface area:volume ratio increases
Carbohydrate Enzyme
Carbohydrase
Protein Enzyme
Protease
Fats Enzyme
Lipids
Examples of Carbohydrase
Amalyse, Maltose
Examples of Protease
Pepsin (found in stomach)
Trypsin (found in small intestines)
What does Carbohydrase break down Carbohydrates into