tertiary and quaternary structure

what are the 2 diffrent types of side chains that can occour

hydrophobic and hydrophillic

whats the effect of the type of side chain called

the hydrophobic effect its a majour driving factor in protien folding and determinant of properties and shit

whats is the hydrophobic colapse

tendancy for hydrophobic molecules to be on the inside while hydrophillic are on the outside

what sort of effect is the hydrophobic collapse

entropic

what is are the types of bonds that can form between side chains

van der wals, hydrogen, disulfide and ion pair

whats the wan der wals interactions between

non covalent bwtween electrically charged neutral molecules - dipoles

what happens between permenant dipoles

the slight bias of charges causes them to attract

whats the diffrence in induced dipoles

similar but inducesd arnt always dipoles they can change

when are van der walls sonly significant

when the atoms are very close

deascribe hydrogen bonding between side chains

bwtween the nitrogen and the oxygen - they are both good hydrogen bond donoes and acceptors

which bond is the strongest

disulfide

explain disulfide bonds between side chains

covalent bonds between 2 cystine side chains

what is an ion pair bond

full electrostatic attraction - asparate and lysine salt bridge

what are ion pair bonds sensitive to

pH

whats the reaction for ionisation

cooh >< coo +h

how is k calculated

{coo}{h}/[cooh]

hpw is pH calculated

pH log10 (h)

what is pka defined as

log 10 ka

what is pka

the pHehere the pair is 50% ionised

what’s the Henderson hassleback equation

ph = pka+log (base)/(acid)

what’s the base in the equation

the proton acceptor

what’s the acid in the reaction

Proton donor

what’s a domain

globular unit within the 3D form that have particular functions

ehat’s the quaternary structure

assembly of more than 1 polypeptide chain

give some examples of quaternary structure protein

haemoglobin, HIV protease