Topic 1 and Topic 2 exam questions Flashcards
- ADD TO IT BY ADDING ABT ACE INHIBITORS ECT (53 cards)
function and structure of LDL (low density lipoprotein)
- saturated fat, protein and cholesterol attached to it
- moves cholesterol from liver to bloodstream
- binds to receptor sites on cell membranes so they can be taken up by cells needed and removes the cholesterol from blood
- high levels of LDL leads to blockage of membrane receptors -> blood cholesterol levels rise
function and structure of HDL (high density lipoproteins)
- unsaturated fat, protein and cholesterol
- transport cholesterol from body tissues to liver, where its broken down
- reduces blood cholesterol + removes fatty plaques that form during atherosclerosis.
what are the two storage polysaccharides and why are they this?
glycogen and starch
- insoluble so have no osmotic effect and they are compact
structure of starch
- amylose: unbranched. 1,4 glycosidic bonds between alpha glucose. helix shape so more compact for storage
- amylopectin: branched. 1,4 and 1,6 glycosidic bonds between alpha glucose. the branches = more terminal gluose = easier to be hydrolysed for use during cellular respiration OR added for storage.
structure of glycogen
- 1,4 and 1,6 glycosidic bonds between alpha glucose
- branched. more branched than amylopectin
- branches = more terminal glucose molecules can be added/removed by hydrolysis
- allows for quick release/storage of glucose = meets needs of cells as animal cells are very metabolically active.
what are the different types of mutations
- deletion
- insertion
- substitution
- duplication
- inversion
what is the result of an insertion
- nucleotide randomly inserted into DNA sequence
- changes amino acid tht would have been coded for by original base triplet as it creates a new diff triplet of bases
- would cause frameshift mutation -> every triplet downstream of the insertion is also changed
- could dramatically change amino acid sequence produced from gene and therefore ability of polypeptide to function
what is result of a deletion mutation
- nucleotide randomly deleted from DNA sequence
- changes triplet in which deletion has occurred and also every grp of 3 bases downstream on deletion (frameshift mutation)
- could dramatically change the amino acid sequence produced and therefore the ability of the polypeptide to function
what is the result of a substitution mutation
when base in dna sequence randomly swapped for different base
- might not alter amino acid at all due to degenerate nature of genetic code (when a single amino acid might be coded for by more than one tripley)
- missense mutation causing it to alter a single amino acid
- nonsense mutation creating a premature stop codon, so polypeptide chain is incomplete, affecting final protein structure and function,
how does change in primary structure cause difficulties in a way an enzyme works
- different primary structure results in a different
sequence of amino acids - this results in change in R groups which changes the {folding / bonding /
secondary structure / tertiary structure } - changing { shape / charge } of the active site prevents
substrate from being able to bind - which means that enzyme no longer can catalyse reaction
what does secondary structure refer to
- relates to hydrogen bonds forming between the amino group and the carboxyl group (the ‘protein backbone’)
what does tertiary structure refer to
- The way that the whole protein folds to make a three dimensional structure.
bonds that form in the tertiary structure
- hydrogen bonds
- ionic bonds
- disulphide bonds (between cysteine amino acids)
- weak hydrophobic interactions between non-polar R groups
quaternary structure
- proteins that have more than one polypeptide chain
- same bonds as in tertiary structure are involved
structure of globular proteins
- compact
- sort of spherical
- non-polar R groups are faced towards centre of protein and polar face outside the protein
- they have specific shapes due to the interactions between the r groups
- some are conjugated proteins with a prosthetic grp
what are prosthetic groups
- permanent non protein part of a protein molecule
function of globular proteins
orientation of R groups means that they are generally soluble in water which means they can be easily transported around organisms and be involved in metabolic reactions
eg:
- enzymes, antibodies, haemoglobin and myoglobin
structure and function of haemoglobin
- globular protein
- oxygen transport molecule
- made of 4 polypeptide chains that each have an iron containing haem group
- oxygen attaches to the iron with the haem group
- its a conjugated protein as its attached to another chemical group
structure of fibrous protein
long chains, do not fold up into a ball shape.
- little to no tertiary structure
- highly repetitive number of amino acid sequences which creates very organised structures
- lots of hydrophobic R groups so insoluble in water
- strong as well, so good for structure
eg: keratin, elastin, collagen
function of fibrous proteins
- they are strong, and insoluble so good for structural molecules.
structure and function of collagen
- fibrous protein
- three polypeptide chains wind around each other and form rope-like strands held together by hydrogen bonds between chains
- each strand cross-links each other to provide tremendous strength.
what are the three ways in which genetic testing can be used
- confirm diagnosis of a certain genetic disease
- to identify carriers so that they can detect abnormal alleles, helping to make informed decision about having children
- for testing embryos
amniocentesis
- insert needle into amniotic fluid
- collect fetal cells that have fallen off foetus and placenta
- carried out around 15-17 weeks of pregnancy and 1% risk of miscarriage
what is chorionic villus sampling?
- remove small sample of placental tissue (which includes cells of embryo or foetus) through abdomen or through vagina
- can be carried out between 8-12 weeks as no need to wait for amniotic fluid to develop
- riskier than amniocentesis.