Biological molecules Flashcards
(39 cards)
Hydrogen bonds in water
- Oxygen attracts the electrons towards itself, becoming slightly negative
- The hydrogen molecules become slightly positive
- Hydrogen bonds form between slightly negative oxygens and slightly positive hydrogens
Hydrogen bonds and properties of water
- good solvent, as can interact with other polar/charged molecules due to hydrogen bonds
- cohesive, as hydrogen bonds stick water molecules together
- density: ice is less dense as hydrogen bonds form a lattice
- high specific heat capacity, as lots of energy is needed to raise the temperature of water
- liquid across a variety of temperatures
Importance of properties of water (6)
- good solvent: metabolic processes rely on chemical reactions occurring in solution
- liquid: good transport medium for transporting materials around organisms
- cohesive: creates surface tension as a habitat and prevents columns of water breaking
- freezing at lower density: water below is insulated (whole lake won’t freeze), provides a habitat
- thermal stability: large bodies of water have fairly constant temperatures, evaporation can cool surfaces
- metabolic: takes part in chemical processes
Structure of amino acids
H H O amino group (NH2)
N C C acid group (COOH)
H R OH R group
Forming peptide bonds
OH (from acid group) and H (from amino group) form water in a condensation reaction. End up with a peptide bond of: l C=O l N-H l
Breaking peptide bonds
Hydrolysis reaction. OH from water goes to C=O (bonds to carbon), H from water goes to N-H
Primary structure
The sequence of amino acids in a polypeptide/protein
Secondary structure
Coiling and pleating (alpha helix and beta pleated sheets) of parts of the polypeptide molecules. Held together by hydrogen bonds between carbon-nitrogen backbone (C=O—-H-N) not between R-groups.
Tertiary structure
Overall 3D structure of the final polypeptide/protein molecule. Held together by: disulfide bonds, ionic bonds, hydrogen bonds, hydrophobic and hydrophilic interactions. Hydrophobic R-groups will be held together with water excluded; hydrophilic groups will be on the outside
Quaternary structure
More than one polypeptide subunit joined together. Protein formed can’t function if not all subunits are present.
Haemoglobin as a protein
- 4 polypeptide subunits
- 1 prosthetic group on each chain: a haem group with Fe2+ ion
- Globular protein: vital tertiary structure
- Soluble in water
- Wide range of amino acids in primary structure
- Many alpha helix structures
Collagen molecule as a protein
- Fibrous protein
- Insoluble in water
- Not much variety in amino acids: 35% is glycine
- No prosthetic groups
- Many left-handed helix structures
Structure of collagen fibres
- Collagen molecules form staggered cross links with adjacent collagen molecules
- This makes collagen fibril
- Many fibrils together become collagen fibres.
Function of haemoglobin
Carry oxygen from lungs to tissues.
Function of collagen
Provide mechanical strength:
- in walls of arteries (no blood bursting from walls)
- tendons of collagen connecting skeletal muscle to bone (muscles can pull bones)
- makes up bones (with other stuff, e.g. calcium phosphate to harden them)
- Cartilage and connective tissue
Structure of alpha glucose
Hexagonal ring, C1, C2, C3, C4, C5, O. C1,2,3,4 have an H and an OH group attached. C5 has C(6)H2OH attached and H. In alpha glucose, the H on C1 is above the plane of the paper (the OH is below the plane of the ring)
Alpha and beta glucose
In alpha glucose, C1 has H above plane of ring and OH below plane of ring. In beta glucose, C1 has OH above plane of ring and H below plane of ring
Forming a glycosidic bond
OH of C1 and H from OH of C4 make a water molecule. The O left on C4 forms the glycosidic bond between C1 and C4. This is a condensation reaction
Breaking a glycosidic bond
OH of a water molecule goes to C1, H of a water molecule binds with the O of the glycosidic bond and forms an OH group on C4. Hydrolysis reaction
alpha glucose + alpha glucose ->
Maltose, a sweet, soluble disaccharide sugar. Forms a glycosidic bond in a condensation reaction
Carbohydrates
Group of molecules containing carbon, hydrogen and oxygen in the ration C(n)(H2O)(n)
Making amylose
Many glycosidic bonds form between many alpha glucoses, forming a long chain of amylose - a polysaccharide.
Starch
Made of amylose and branched amylopectin (when C1 - C6 bond forms). Energy-storage molecule for plants. Stored in chloroplasts and in membrane bound starch grains. Can be broken down into glucose molecules for respiration. Insoluble, so doesn’t effect water potential.
Amylose
Long chain of many alpha glucoses glycosidically bonded together. Long chain coils up into a compact molecule; iodine can become trapped in the coils of the spring, causing iodine in potassium iodide change colour (starch test)