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phi = -130, psi = +130

pleated to allow closer approach for hydrogen bonding between sheets
may be parallel or anti-parallel with anti-parallel arrangements being more stable by
allowing closer approach for hydrogen bonding
have right hand twist
alternating residues of side chains point outwards to different sides of the sheet; this allows
sheets to have one hydrophobic side, and one hydrophilic side !his allows water to be
e"cluded from the core while still allowing the protein to be soluble
#omposed always of 1+ sheets that hydrogen bond to each other
$lpha helices
!he ith residue of an alpha heli" forms a bac%bone-bac%bone hydrogen bond with the i+&

residue in the heli" !his involves the amino group acting as the hydrogen bond donor and
the carbonyl acts as the acceptor
phi = -'(, psi = -&(
consecutive residues alternate with their side chains pointing outwards from the helical a"is
on different sides, at a slightly upward angle !his allows one side to be hydrophobic and
one to be hydrophilic, and for water e"clusion
!he heli" is right handed with a turn of 100 deg per residue; each full turn occurs every '&$
which e)uates to 1'$ per residues
!his phenomena gives rise to a heptad repeat pattern, where if a residue is ta%en to be the ith
residue, the i+3
residue will be appro"imately on the same side of the heli" !his allows for
hydrophobic residues to be lined up
*lectrostatic interactions+
,ue to opposite charges on interacting residues
!hese charges are generally localised over several atoms
$lso called a salt bridge
$ component due to electrostatic forces, another due to hydrogen bonding
Between acidic residues -asp, glu. and basic residues -lys, his, arg.
/on polar interactions+
/on polar proteins do not interact with water well, causing water to form a cage of sorts
around them -hydrophobic effect.
!his is entropically unfavourable
0olding of the protein or interactions between non polar groups causes e"clusion of water
from the non polar core, this releases some water molecules and results in an entropic
driving force for folding1non polar interactions
#ause by dipoles by polar groups interacting between molecules
#ould be between atoms with a high difference in electronegativity -permanent dipole. or
simillarly negativities -instantaneous induced dipoles.
4ydrogen bonding can be thought of as an e"treme case of 2,3 interactions as hydrogen is
very electropositive and acceptor atoms are very electronegative -5, 0 and /.
,ipoles in a molecule can add up to give a dipole moment
!ransmembrane proteins
Beta barrels may form pores #onsist of one sheet folded around so that the ends hydrogen
bond with each other ,ue to the fact that side chains for consecutive residues alternate
between each side of the sheet, the inside of the pore can be hydrophilic but the outside
hydrophobic -allowing it to be embedded in the membrane.
4elices+ 60-30 residues to span a membrane, protein-protein and protein-lipid interactions,
mediated by hydrophobic side chains
7esides that are in the membrane are mostly non polar
!yr1!rp found at the interface between polar and non polar acyl chain and head 4ydrophilic
residues in solvent e"posed loops #ystoplasmic side -vely charged and positively s%ewed
#holesterol upta%e via endocytosis using clathrin coated pits then vesicles into cell
defective receptors for 8,8 adaptins can cause 8,8 build up in blood and atherosclerosis
*arly endosome is the main sorting station for the pathway 9 low p4 of : allows the 8,8 to
dissociate from its receptor
7eceptors go into vesicles which undergo e"ocytosis to return as part of membranes
2esicles with lipases from golgi ;oin early endosome and cholesterol is degraded
#holesterol can cross the membrane of what is now lyso<ome into main part of cell
0ocal $dhesions
!alin activated by 7!=1> protein, causes intergin to straighten and engage *#?
8in%s to actin cytos%eleton which allows cell attachment to substrata
*#?-integrin interactions are important in generating cell traction forces allowing for
0ocal adhesions are sites of anchorage for actin with *#?, also concentrate signalling
@nside out signalling+
7!=1>-protein activates talin which causes integrin to engage *#?
>rowth factor receptor signal activates integrins via intracellular signalling
talin activates integrin by binding intracell beta domain
5utside in signalling+
*#? binding recruits proteins that recruit %inases
?ultiple integrins recruited to focal adhesions to concentrate signals
$ctin is concentrated
integrins dont have %inase activity, recruit eg 0$=
0$= signals through ?$A= for proliferation, others for survival, motiliy and disassembles
0$Bs C metastasis
Dtable epithelium+
#ells intimately connected to each other
$pico-Basal polarity
8ittle *#?
Aroliferation balances death
#ontrolled responses to growth signals1anti-growth signals
/o blood vessels or connective tissue
$dhesive *#? proteins+
?ultiple binding domains
0ibronectin dimers form fibrils by binding an 7>, se)uence on integrin, tension causes
e"posure of cryptic binding sites where fibrils can grow *ssential for cell migration eg
neural crest cells
8aminin is made of 3 chains -alpha, beta, gamma. lin%ed by disulfide bonds ?ultiple
binding domains, bind to other *#? components and basal lamina =noc%out causes
muscular dystrophy
!ension on integrins may combine with growth factor signalling in order to promote cell growth
@ntegrins = mechanoreceptors
@nsulin, glucagon, adrenaline
allosteric regulation
heptad repeat diagram
= 7$D