Biological Molecules Flashcards
what are the five biological molecules we learn about
-water
-carbohydrates
-proteins
-nucleic acids
-lipids
how do hydrogen bonds form between water molecules
-water=polar: O is more electronegative than H, so attracts electron density in covalent bonds more strongly. O=slightly neg. H=slightly pos
-intermolecular forces of attraction between a lone pair on O of one molecule and H on an adjacent molecule.
state 7 biologically important properties of water
-ice=less dense than water, reaches max density at 4°C
-high surface tension
-incompressible
-solvent
-high specific heat capacity
-high latent heat of vaporisation
-cohesion between molecules
Why is latent heat significant
-large amount of TE is absorbed to break hydrogen bonds and evaporate water.
-little water is required to evaporate in order for organisms to lose lots of energy- provides a COOLING effect.
-e.g sweat or transpiration
why is the incompressible nature of water important
-provides turgidity
-provides hydrostatic skeleton for some small animals, e.g earthworms
why does ice float on water and importance
-H-bonds hold molecules in fixed positions further away from each other.
-insulates water in arctic climates so aquatic organisms can survive. layer of water will freeze in extreme temps and rise to the top, reducing heat loss and preventing the whole body of water freezing.
high surface tension of water importance
-slows water loss due to transpiration in plants
-water rises unusually high in narrow tubes, lowering demand on root pressure
-some insects can ‘skim’ across the surface of water.
water as a solvent importance
polar universal solvent dissolves & transports charged
particles involved in intra & extracellular reactions e.g PO4 3- for DNA synthesis.
high specific heat capacity and latent heat of vaporisation importance
-acts as a T buffer, enables endotherms to resist fluctuations in core T to maintain optimum enzyme activity.
-cooling effect when water evaporates from skin surface as sweat/from mouth when panting.
define monomer
smaller units that join together to form larger molecules
examples of monomers
-monosaccharides (glucose, fructose, galactose, ribose)
-amino acids
-nucleotides
define polymer
molecules formed when many monomers join together
examples of polymers
-polysaccharides
-proteins
-DNA / RNA
what happens in condensation and hydrolysis reactions
-condensation= chemical bond forms between 2 molecules & a molecule of water is produced.
-hydrolysis= water molecule is used to break a chemical bond between 2 molecules e.g. peptide bonds in proteins, ester bonds between fatty acids and glycerol in lipids
name the elements found in carbohydrates, lipids, proteins, and nucleic acids.
carbohydrates & lipids= C H O
proteins= C H O N S
nucleic acids= C H O N P
structure of alpha and beta glucose
alpha= hydrogen above
beta=hydrogen below
properties of alpha glucose
-small & water soluble= easily transported in bloodstream
-complementary shape to antiport for co-transport for absorption in gut
-complementary shape to enzymes for glycolysis=respiratory substrate.
what bond forms when monosaccharides react
glycosidic
name 3 disaccharides and how they form
-maltose= glucose + glucose
-sucrose= glucose + fructose
-lactose= glucose + galactose
all have molecular formula C12H22O11
describe structure and function of starch
storage polymer of alpha glucose in plant cells
-insoluble=no osmotic effect on cells
-large=does not diffuse out of cells
made from amylose:
-1,4 glycosidic bonds
-helix with intermolecular H-bonds=compact
and amylopectin:
-1,4 & 1,6 glycosidic bonds.
-branched= many terminal ends for hydrolysis into glucose.
describe structure ad functions of glycogen
main storage polymer of alpha glucose in animal cells (also found in plants)
-1,4 & 1,6 glycosidic bonds
-branched= many terminal ends for hydrolysis
-insoluble= no osmotic effect & doesn’t diffuse out of cells
-compact
describe structure and function of cellulose
polymer of beta glucose gives rigidity to plant cell walls (prevents bursting under turgor pressure, holds stem up)
-1,4 glycosidic bonds
-straight-chain, unbranched molecule
-alternate glucose molecules are rotated 180
-H-bond crosslinks between parallel strands form microfibrils=high tensile strength.
how do triglycerides form
condensation reaction between 1 molecule of glycerol & 3 fatty acids which form ester bonds.
compare saturated and unsaturated fatty acids
saturated:
-single C-C bonds only
-straight-chain lots of contact points
-higher melting point=solid at room T
-found in animal fats
unsaturated:
-contain C=C bonds
-‘kinked’ molecule have fewer contact points
-lower melting point=liquid at room T
-found in plant oils
relate the stucture of triglycerides to their function
-high energy:mass ratio= high caloric value from oxidation (energy storage)
-insoluble hydrocarbon chain = no effect on water potential of cells & used for waterproofing
-slow conductor of heat= thermal insulation e.g adipose tissue.
-less dense than water = buoyancy of aquatic animals.
describe the structure and function of phospholipids
amphithatic: glycerol backbone attatched to 2 hydrophobic fatty acid tails & 1 hydrophilic polar phosphate head.
-forms phospholipid bilayer in water = component of membranes
-tails can splay outwards = waterproofing e.g for skin
are phospholipids and triglycerides polymers
no, they are macromolecules.
-not made from a small repeating unit.
structure and function of cholesterol
-steroid structure of 4 hydrocarbon rings. Hydrocarbon tail on one side, hydroxyl group (-OH) on the other.
-adds stability to cell surface phospholipid bilayer by connecting molecules & reducing fluidity.
general structure of an amino acid
- COOH carboxyl
-R variable side group
-NH2 amine group
how do polypeptides form
condensation reactions between amino acids form peptide bonds (-CONH-)
4 levels of protein structure
define primary and secondary structure of a protein
primary- sequence, number & type of amino acids in the polypeptide, determined by sequence of codons on mRNA.
secondary- weak negatively charged N and O interact with weak positively charged H to form hydrogen bonds
describe the 2 types of secondary protein structure
a-helix:
-all N-H bonds on same side of protein chain
-spiral shape
-H-bonds parallel to helical axis
B-pleated sheet:
-N-H & C=O groups alternate from one side to the other
define tertiary structure of protein and bonds present
3D structure formed by further folding
-Disulphide bridges: strong covalent S-S bonds between molecules of the amino acid cysteine.
-Ionic bonds: relatively strong bonds between charged R groups (pH changes cause these bonds to break)
- hydrogen bonds: numerous & easily brokenn
define quaternary structure of a protein
-functional proteins may consist of more than one polypeptide.
-precise 3D structure held together by the same types of bond as tertiary structure
-may involve addition of prosthetic groups e.g metal ions or phosphate groups