Biological Molecules
Biological Molecules
<aside> š” Monomer: A building block, usually referring to the same type of āblockā that makes up something larger
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Carbohydrates:
Provide energy and structural support(Cell wall)
All carbohydrates include carbon, hydrogen and oxygen.
Fiber is a carbohydrate that prevents constipation
Foods: Breads, cereals, vegetables, fruits and seeds
Extra glucose is converted into glycogen in the liver
Three types of Carbohydrates
The monomer of a carbohydrate is the monosaccharide - 1 sugar
Plants have cell walls of carbohydrates, specifically a large one known as cellulose
Fungi also have cell walls of carbohydrates, it is known as chitin
Examples:
Glucose: Bread, rice and pasta(Glucose is also used to make ATP)
Because of that, it makes carbohydrates a fast source of energy for cells.
Fructose: Fruits
Galactose: Vegetables and dairy
Disaccharide - 2 sugar (Two monosaccharides combined together by a glycosidic bond):
Monosaccharide + Monosaccharide = Disaccharide
Maltose: Glucose and glucose
Sucrose: Glucose and fructose
Polysaccharides - More than 10 sugars (more than two monosaccharides combined together by a glycosidic bond)
Starch: Glucose, amylose and amylopectin
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<aside> š” Dehydration Synthesis - Two monomers joining together by removing a water molecule Hydrolysis - Two monomers disconnecting by adding a water molecule
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Disaccharide | Monosaccharide | Found in |
|---|---|---|
Maltose | glucose + glucose | Germinating seeds |
Sucrose | glucose + fructose | Sugar cane (table sugar) |
Lactose | glucose + galactose | Milk |
If you continue joining together monosaccharides with glycosidic bonds you can make very long chains of sugars
They are perfect for storing sugar in a cell because they are insoluble so do not affect water potential in the cell
Lipids(Fats, Oils)
<aside> š” Saturated fats - single bonds connecting elements, extremely packed
Unsaturated fats - mixture of single and double bonds connecting elements, less packed
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Lipids are a diverse group of compounds that are insoluble in water but soluble in organic solvents such as ethanol
One thing lipids generally share is that they contain a hydrophobic component. Essentially, they dislike water. Which means they wont dissolve in water
Lipids have a major function of being a source of long term energy storage
When carbs are used up, lipids are also very important as a long term energy source that an organism can use.
Cell membrane structure is made from lipids
The monomer for lipids are glycerol and fatty acids
The most common types of lipids are triglycerides (sometimes known as true fats or neutral fats), but other important lipids include waxes, steroids and cholesterol.
Like carbohydrates, lipids contain carbon, hydrogen and oxygen, but they have a higher proportion of hydrogen and a lower proportion of oxygen.
Connected by fatty acids
Proteins
Proteins are a diverse group of large and complex polymer molecules, made up of long chains of amino acids (20 types)
They have a wide range of biological roles, including:
Structural: Proteins are the main component of body tissues, such as muscle, skin, ligaments and hair
Catalytic: All enzymes are proteins, catalyzing many biochemiical reactions
Signalling: Many hormones and receptors are proteins
Immunological: All antibodies are proteins
All amino acids have the same general structure: the only difference between each one is the nature of the R group. The R group therefore defines an amino acid
The R group therefore defines an amino acid (determines the type of amino acid) .
The R group represents a side chain from the central āalphaā carbon atom, and can be anything from a simple hydrogen atom to a more complex ring structures.
Essential Amino Acids:
histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine
Non Essential Amino Acids:
alanine, arginine, asparagine, aspartic acid (aspartate), cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine
Amino Acid + Amino Acid = Dipeptide + Dipeptide = Peptides
Dipeptides = Two amino acids
Peptides = Two dipeptides
Polypeptide = long unbroken chain of peptides (broken is peptide chain)
(Complex) Proteins = One of more polypeptide chains folded into a highly specific 3D shape
All of the bond between amino acids are called peptide bonds
Role | Examples | |
|---|---|---|
Hormones | Quicken chemical reactions | Sucrase: Positions sucrose (table sugar) ijn such a way that it can be broken down into component parts of glucose and fructose. |
Transport | Chemical messengers | Growth hormone: stimulates growth of bones |
Contractile | Move other molecules | Hemoglobin: Transports oxygen through blood |
Protective | Movement | Myosin and actin: Allows muscles to contract |
Structural | Healing; defense against invaders | Fibrinogen: Stops bleeding |
Antibodies: Kill bacteria invaders | ||
Storage | Mechanical support | |
Toxins | Stores nutrients | |
Communication | ||
Enzymes |
When more amino acids are added to dipeptide, a polypeptide chain is formed
A protein consist of one or more polypeptide chains folded into a highly specific 3D shape.
There are up to four levels of structure in a protein: primary, secondary, tertiary and quaternary. Each of these play an important role in the overall structure and function of the protein
Type of Structure | Description |
|---|---|
Primary | polypeptide chain |
Secondary structure | polypeptides in coils or sheets |
Tertiary | coils or sheets form a tangle |
Quaternary | more than one tangle combine to make a very completed protien |
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Types of protein structures
Fibrous Proteins
Fibrous proteins are formed from parallel polypeptide chains held together by cross-links. These form long, rope-like fibres, with high tensile strength and are generally insoluble in water.
Collagen-the main component of connective tissue such as ligaments, tendons and cartilage
Keratin-the main component of hard structures such as hair, nails, claws and hooves
Silk-forms spiders webs and silkworms cocoons
Globular protiens
Globular proteins usually have a spherical shape caused by tightly folded polypeptide chains.
The chains are usually folded so that hydrophobic groups are on the inside, while the hydrophilic groups are on the outside. This makes many globular proteins soluble in water.
Transport proteins-such as hemoglobin, myoglobin and those embedded in membranes
Enzymes-such as lipase and DNA polymerase
Hormones-such as oestrogen and insulin
Denaturing proteins
If the bonds that maintain a proteinās shape are broken, the protein will stop working properly and is denatured.
Changes in temperature, pH or salt concentration can all denature a protein, although the specific conditions will vary from protein to protein
Fibrous protein lose their structural strength when denatured, whereas globular proteins become insoluble and inactive.
DNA (Deoxyribonucleic Acid)
Was discovered by Watson and Crick
A-Adenine
G-Guanine
T-Thymine (U - Uracil, for RNA only)
C-Cytosine
DNA (Deoxyribonucleic acid) directs & controls all activities of all cells in an organism - RNA (Ribonucleic acid) helps
DNA ā RNA ā Protein
DNA: A, G, T, C
RNA: A, G, U, C
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DNA Structure:
Made up of nucleotides
Sugar, phosphate, nitrogenous base
Polymers (chain of units): DNA (deoxyribonucleic acid, double helix, found in humans) or RNA (single helix, normally found in bacteria)
Base paring rule (complementary):
Adenine always binds with Thymine (A - T) (Purines, 2-H bonds)
Guanine always binds with Cytosine(G - C) (Pyrimidines, 3-H bonds)
Connected to each other through phosphodiester bonds
Nucleic Acids
Atoms: Carbon, Hydrogen, Oxygen, Phosphorus and Sulphur
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Digestion Products
Macromolecule Eaten | Broken Down in Stomach to: |
|---|---|
Carbohydrates | Simple sugars (i.e. glucose) |
Lipids | Fatty acids and glycerol (glycerol further broken down to glucose) |
Proteins | Amino Acids |
Nucleic Acids | Nucleotides |
Alkaline substance mixed with oil lets it mix with water