Unfamiliar concepts - Flashcards
Waters polarity -
Because the negative shared hydrogen electrons are pulled towards the oxygen atom, the other side of the hydrogen is left with a positive charge.
Why ice is less dense -
Hydrogen bonding
fix positions of the molecule slightly further apart, producing a giant rigid open structure (oxygen is at the centre)
Cohesion and adhesion -
Cohesion (coperative) attraction between the same molecule due to its polarity
Adhesion when water molecules are attracted to other materials.
Golgi and ER = (Cristernae or Cristae)
Mitochondria =
G and ER = cristernae
Mito = cristae
Protein Production -
1Ribosomes come from nucleolus leave through pores as are small,
2 Pass into cristernae and packaged into transport vesicles
3 contain newly synthesised proteins which move to the cytoskeleton
4 Vesicles fuse with the cis face on the golgi, structurally modified
5 secretory vesicles fuse with the membrane exocytosis lysosomes stay inside the cell
Flagella difference between euk and prok -
P - made up of protein filaments when present arranged in helix.
E - made up of microtubules proteins in a 9+2 formation
Glucose structure -
Glucose = c6 h12 o6
oh and h swapped between alpha and beta
Middle swapped, outside same of OH and H groups (observe in book)
Left top CH2OH
Glycosidic bonds are what and created how?
Covalent bond
Condensation
Formed by the reaction of hydroxyl groups, existing bonds are broken.
Monosaccharide - examples
Glucose, fructose and galactose
Disaccharide examples -
Sucrose, lactose and maltose
Polysaccharide examples -
Glycogen, starch, cellulose
Ribose structure -
Pentose similar structure to beta glucose
Starch -
Mixture of two alpha glucose polysaccs
Amylase (UB) = 1-4 gly bonds, angle of bonds forms an insoluble helix, stabilised by hydrogen bonds, good for storage
Amylopectin (B) = 1-4, 1-6 gly bonds, two glucose molecules, giving it a branched structure, enzymes can reach the branches quicker to break down the gly bonds releasing glucose, insoluble
Glycogen -
Main energy source in animals, similar structure but has way more branches that the starch one, coiling and branching = storage, end branch is free meaning glucose can be removed and added, has more branches due to metabolism, alpha glucose
Cellulose -
Plant cell walls - Hydroxl groups on 1 and 4 are too far to reach, turning to a beta glucose aswell can join the reaction together.
Lipids polar or non-polar
Non-polar, due to the electrons being more evenly distributed than in polar molecules meaning there is no reasons of positivity or negativity
Lipids are large MM?
Macromolecules, which are not built for repeating units.
Triglyceride formation -
One glycerol and three fatty acids
Glycerol belong to which group -
Alcohols
Fatty acids belong to which group -
Carboxylic acids
The process of triglycerides synthesising is and how many water molecules are formed -
Esterification and 3 water molecules
Saturated fatty acids -
Do not have double bonds present between carbon molecules, general structure is CnH (2n+1) COOH
Unsaturated fatty acids
Have double bonds between carbon atoms present , one being monosaturated, you get the picture with the others. This allows the molecule to bend and be packed closely together, liquid at room temperature
Phospholipids -
These are modified triglycerides, inorganic ions are found in the cytoplasm of every cell and so negatively charged makes them soluble in water. Contain two fatty acid tails
Phosphate heads in the bilayer -
Polar and hydrophilic
Fatty acids in the bilayer -
Non-polar and hydrophobic
Cholesterol -
A sterol and important in the phospholipid bilayer, complex alcohol molecules, its positioned between the phospholipids, adds stability and keeps fluidity at low temperatures and stops them from becoming too fluid at higher temperatures.
General amino acid structure -
R Variable group
A group H2N - C - COOH Carboxyl group
H
What catalyses the peptide bonds forming -
Peptidal transferase present in the ribosome for the site of protein synthesis (translation)
Value of R groups in an amino acid -
Able to interact with each other, forming different types of bonds leads to long chains of polypeptides
Primary structure of a protein -
Peptide bonds and the sequence of amino acids, the particular amino acids will influence how the polypeptides fold to give the final shape.
Secondary structure of a protein -
Hydrogen bonds begin to form changing the initial folding of the polypeptide chain, start coiling, the oxygen, hydrogen and nitrogen atoms of the amino acid interact.
Tertiary structure of protein structures -
Overall 3D shape and ionic bonds, results in more bonds between the polypeptide chain, coiling or folding of secondary structures brings in the R group brings it closer together. Phillic and phobic reactions between polar and non-polar R groups, ionic bonds are stronger than H bonds and form between opposite charged R groups, disulfide bridges form between opposite R groups of proteins with some atoms that contain sulfur atoms.
Quaternary structure of proteins -
Involves the interactions of two or more subunits of alpha or beta, interactions same as tertiary, but between different protein molecules E.G Insulin has 2 subunits and haemoglobin has 4 subunits 2 the same.
Globular proteins -
Compact and water soluble, roughly spherical in shape, formed when they fold into their tertiary structures. Hydrophilic R groups are pushed outwards, hydrophobic R groups are pushed inside away from the aqueous environment.
Insulin as a globular protein -
Regulate blood glucose, in the pancreas, soluble in the bloodstream, needs precise shape to fit receptors, contains two polypeptide chains held by disulfide bridges.
Conjugated proteins -
Globular proteins which contain a non-protein part attached to them called a prosthetic group. Haem groups contain Iron ions Fe 2+
Haemoglobin as a conjugated protein -
Quaternary, made up of 4 polypeptides, two alpha and beta subunits, the Iron Ions are able to combine reversely with oxygen molecule, enables oxygen to be transported around the body.
Fibrous proteins -
Long chains of insoluble molecule, keratin, elastin and collagen tend to be strong, structural and unreactive proteins, not associated with long 3D complex shapes.