BCM10 Flashcards
average length of peptide
40aa
what is conformation?
curvature in 3d space
what is phi
rotation around N- C alpha bond
what is psi
rotation around c alpha c bond
what do phi and psi look like
phi - ϕ
psi - Ψ
what is omega
rotatation around C-N bond not allowed
resonance
omega is 180 degrees for trans
what is the main chain conformation defined by?
sequence of phi and psi angles
what is a ramachandaran plot
shows allowed phi and psi angles
for all aa apart from glycine
only certain combos of tortion angles allowed
+psi - phi
antiparrallel beta sheets
parallel beta sheets
+psi +phi
left handed helix
- psi -phi
alpha helix
what does the secondary structure entail?
h bonding
alpha helix
beta pleated sheets
what did lineus pauling and robert carey discover?
xray diffraction
Using standard length and bond angles
proposed beta pleated sheet and alpha helix
describe right handed helix
all main chain co and nh are bonded.
side chains are extended outwards
3.6 angstrums per turn
1/5 angrstrum rise
what does hydrogen bonding happen between?
carbony of ith residue and nitrgoen of i+4 th residue
what is the optimal distance for hydrogen bonding?
2.8 angstrums
describe beta pleated sheet
2.4 angrstrums per residue
side chains point alternatively up adn down
stabilised by main chain main chain nh/co h bonds
adjacent strands
h bonds between nh/co groupsa re far apart in aa sequence
insdie is hydrophoci
outside is hydrophillic
how is tertiary strucutre held together?
by hydrophobic interactions and h bonds
how do polar and charged amino acids interact?
via h bonds and ionic interaction
- gather on outsdie adn interact with water molecules
what helps stabilise some 3d tertiary protein structures?
ss bonds and metal ions
what are tertiary strucutres used to work out?
evolutionary origins
what do oligimers usually exhibit?
rotational symmetry
dimers trimer penatmers etc
give 2 examples of oligimers with rotational symmetry
lysal trna synthetase = 2 fold axis
groel = 7 fold axis
describe alpha keeratin
alpha helical coiled coil
140A
left handed supercoil
hydrophobic residues clipping together
describe the secondary tertiary and quaternary structure of haemoglobin
2 - alpha helix in parts
3 - metal ion stabilisation
4- hetero multimer