BCM10 Flashcards

1
Q

average length of peptide

A

40aa

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2
Q

what is conformation?

A

curvature in 3d space

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3
Q

what is phi

A

rotation around N- C alpha bond

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4
Q

what is psi

A

rotation around c alpha c bond

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5
Q

what do phi and psi look like

A

phi - ϕ

psi - Ψ

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6
Q

what is omega

A

rotatation around C-N bond not allowed
resonance
omega is 180 degrees for trans

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7
Q

what is the main chain conformation defined by?

A

sequence of phi and psi angles

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8
Q

what is a ramachandaran plot

A

shows allowed phi and psi angles
for all aa apart from glycine
only certain combos of tortion angles allowed

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9
Q

+psi - phi

A

antiparrallel beta sheets

parallel beta sheets

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10
Q

+psi +phi

A

left handed helix

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11
Q
  • psi -phi
A

alpha helix

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12
Q

what does the secondary structure entail?

A

h bonding
alpha helix
beta pleated sheets

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13
Q

what did lineus pauling and robert carey discover?

A

xray diffraction
Using standard length and bond angles
proposed beta pleated sheet and alpha helix

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14
Q

describe right handed helix

A

all main chain co and nh are bonded.
side chains are extended outwards
3.6 angstrums per turn
1/5 angrstrum rise

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15
Q

what does hydrogen bonding happen between?

A

carbony of ith residue and nitrgoen of i+4 th residue

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16
Q

what is the optimal distance for hydrogen bonding?

A

2.8 angstrums

17
Q

describe beta pleated sheet

A

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

18
Q

how is tertiary strucutre held together?

A

by hydrophobic interactions and h bonds

19
Q

how do polar and charged amino acids interact?

A

via h bonds and ionic interaction

- gather on outsdie adn interact with water molecules

20
Q

what helps stabilise some 3d tertiary protein structures?

A

ss bonds and metal ions

21
Q

what are tertiary strucutres used to work out?

A

evolutionary origins

22
Q

what do oligimers usually exhibit?

A

rotational symmetry

dimers trimer penatmers etc

23
Q

give 2 examples of oligimers with rotational symmetry

A

lysal trna synthetase = 2 fold axis

groel = 7 fold axis

24
Q

describe alpha keeratin

A

alpha helical coiled coil
140A
left handed supercoil
hydrophobic residues clipping together

25
Q

describe the secondary tertiary and quaternary structure of haemoglobin

A

2 - alpha helix in parts
3 - metal ion stabilisation
4- hetero multimer