Biological Molecules Flashcards
Macronutrient
Organic compounds required in large amounts
- Proteins
- Lipids
- Carbohydrates
Protein
An organic macromolecule essential to life.
Formed from one or more polypeptides
Enzymes
Globular proteins that act as biological catalysts to increase the rate of reactions
Uses of protein
Enzymes which catalyse chemical reactions
- Forming muscle, bone and other structural features
- Emergency energy source
Elements in protein
- Carbon
- Hydrogen
- Oxygen
- Nitrogen
- Other elements like iron and sulphur
Condensation reaction
When 2 molecules join together, with water as a byproduct
Hydrolysis reaction
When 2 molecules break apart when water is added
Bonding of protein
- Peptide bonds between amino acids
- Regular covalent bonds within the amino acid
- Ionic, hydrogen, disulfide, or hydrophobic bonds on secondary and tertiary levels
Hydrogen bond
A weak interaction between a negative ion and a positive hydrogen atom
Covalent bond
A strong interaction resulting in the sharing of electrons in the outer shell.
E.g. disulfide, phosphodiester, peptide, glycosidic
Cyclic form
The shape formed by a molecule where the final atom is attached to the first
Straight line form
The shape formed by a molecule where all the atoms are in a line
Amino acid
A monomer of proteins with 20 different types
- Amphoteric and a buffer
- Composed of the same basic structure, but with a unique R group
Amphoteric
A compound that is able to react with both bases and acids.
E.g. Amino acids, water, hydrogen carbonate ions
Peptide bond
A strong chemical bond between two amino acids, formed through a condensation reaction.
- When aqueous, the amino group goes from NH₂ to NH₃⁺ (+H⁺)
- The Carboxyl group goes from COOH to COO⁻ (-H⁺)
- The carboxyl and amino acids then bind, with water as a byproduct
Amino acid structure
- Hydrogen group
- Amino group
- Carboxyl group
- R group / side chain
Carboxyl group
- COOH
- Acidic
- Found in single bonded monosaccharides
- Found in amino acids
Dipeptide
Two amino acids that have combined together with a condensation reaction between the amino and carboxyl groups, resulting in the release of water
Polypeptide
A chain of multiple amino acids
Primary structure
The order of amino acids in a protein.
Has peptide bonds between amino and carboxyl groups
Secondary structure
When chains of amino acids coil or fold
36 amino acids per 10 turns
- Two different types: α-helix, β-pleated sheet
- Lots of hydrogen bonds between -NH group and -CO group further down the chain
- Stable at optimal temperatures
Alpha helix
A form of secondary structure of amino acids where the amino acids that bind are 4 places apart. Resulting in a twirl shape
Beta pleated shee
A form of secondary structure where a zig-zag structure is formed as the chains folds over itself
Tertiary structure
When coiled chains of amino acids are folded into precise shapes, usually either supercoiled or spherical.
Mostly exhibited in globular proteins, with fibrous proteins often stopping at secondary structure
- Variety of bonds, including ionic, hydrogen,hydrophilic, hydrophobic, disulfide
Ionic bonds
Bonds formed between oppositely charged groups on amino acids. Formed in tertiary structures
Disulfide bonds
A bond between the sulfide components of the R-group of cysteines.
A form of strong covalent bonds
Quaternary structure
A combination of multiple polypeptide chains.
Almost exclusively found in globular proteins
Fibrous proteins
A form of tertiary structure of proteins where the chains of amino acids are arranged in long patterns.
Usually insoluble in water
Examples of fibrous proteins
- Keratin
- Collagen
- Elastin
Collagen
A fibrous protein where every 3rd amino acid is glycine, giving strength due to the small size of glycine.
- Composed of 3 chains of around 1000 amino acids each. Bonded with hydrogen bonds
- Structural protein that gives strength to skin, bones, tendons and forms cartilage.
- Found in artery walls, bones, and connective tissue
Keratin
A fibrous protein rich in cysteine, with lots of disulfide bridges
- Strong, waterproof, barrier
- Found in hair, nails, claws, hoofs
Elastin
A fibrous protein with many cross-links and coils to give strength and elasticity
- Found in skin, lungs, bladder, blood vessels
Globular protein
A protein of a roughly spherical shape.
- Hydrophobic parts are towards the centre, and hydrophilic towards the surface, making the protein water soluble.
- Often have very specific shapes
Examples of globular proteins
- Haemoglobin
- Insulin
- Pepsin
- Most enzymes
Conjugated protein
A protein to which another chemical is attached
E.g. glycoprotein, lipoprotein
Haemoglobin
A globular protein formed from 2 alpha and 2 beta chains, each with a haem group attached.
- Held together in a specific shape
Insulin
A globular protein made of 2 polypeptide chains, with both alpha and beta folding
- Soluble to water
- Increases the uptake of glucose in the liver
Pepsin
A globular protein made up of a single polypeptide chain of 327 amino acids
- Able to work in acidic conditions due to the high proportion of acidic R groups compared to basic R groups
- Breakdowns enzymes in the stomach
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Biuret test
A qualitative test for proteins
Carbohydrate
A compound made of carbon, hydrogen and oxygen. Also a form of macronutrient that is the primary energy source for humans
Elements in carbohydrates
- Carbon
- Oxygen
- Hydrogen
Uses of carbohydrates
- Primary energy source of humans
- Structural units
- Energy store