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what are the 2 types of secondary structure
alpha helix and beta sheets
decsribe the structure of an alpha helix
like a coil, right handed helix
how many residues
3.6 residures each turn
what do the 3.6 residues per turn mean for the side chains
they are all at 100 degrees from eachother
what bonds are presnent and where are they
hydrogen bonding within the backbone residues
which directions do the side chains project from, what does this allow
outwards, allows them to interact with other things
what do the hydrogen bonds form
cross turns
whats the rule for cross turns
n - n+4 links (1 in bound to 5, 2 is bound to 6 ect)
what do the cross turns result in
stabilisation of the aplha helix
what are helix formers, give example
amino actids that are likly to form alpha helix, glutamate
what are helix destabalisers, give example
aa. that can be in alpha helixes but if theres lots of them they will disrupt, tyrosine
what are helix breakers
theyre almost never found in alpha helixes, proline
why are helix breakers never found in alpha helixes
the r group has bonded back to the amino acid so none of the bonds can rotate(phi bond)
what are th 2 types of beta pleated sheets
parralel and anti parralell
whats the structure of the antiparralel strand
c to n and then n to c
where does the hydrogen bonding occour in the antiparrallel sheets
between the o and the h, relitivly straight bonds
what does the hydrogen bonding allow for
more thn 2 sheets to be involved- some protiens have extensive numbers of sheets
whats an example of anitparralel beta sheets
silk- repetitive of glycine and alanine
where are the r groups on the sheets
up and down away form the sheet
whats the formation of parralel pleated sheets
n to c and n to c
what does the structure of the parallel sheet result in
less strenghts as the bonds arnt straight
where does the hydrogen bonding occour in all secondary structures
between backbons and backbone
what is a structural motife
arrangement of the secondary structures repetedly