Proteins 2 Flashcards

1
Q

How is h bonding formed in an alpha helix (secondary protien structure)

A

The c=o of residue i accepts a H bind from residue i+4

The c=o from i+1 accepts from the nh of i+5

This makes a bend

These residues are all in a chain but then make the alpha helix due to h binding within the structure

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2
Q

What are the alpha helix phi and psi angles on ramachandran

A

-60,-60

The c=o groups point away and nh point forward

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3
Q

In an alpha helix structure, what is the confirmation of all of the c=o

A

They all point down in the structure

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4
Q

In an alpha helix are all c=o and amide groups h bonded to each other

A

All are except for the residue at the top and bottom ends of the helix

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5
Q

What type of shape represents the polypeptide main chain

What is sticking out

What direction and handedness is the structure

A

A ribbon

The r groups stick out

The ribbon is going CW. Means it’s right handed because if going cw with right hand the thumb faces down to the C terminus

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6
Q

What is the rise per residue of the alpha helix

What is the rotation per residue

So how many residues per rotation?

A

From one alpha c to another the rise is 1.5 A

the rotation is 100 degrees

360/100 degrees is 3.6 residues per rotations

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7
Q

What is special about the ribbon and cylinder depiction of the alpha helix

A

They both ignore the side chains that stick out of the helix

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8
Q

What do the tubes that follow the alpha helix represent

A

Is represents the path of the polypeptide chain when it’s not forming an alpha helix

The atoms in these tube are just primary peptides

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9
Q

How are beta sheets formed

A

Because the main chain has h binding potential, another chain can come in antiparallel and do h bonding interactions between the c=o and NH directly across from each other

The r groups alternate in and out

This causes the beta sheet

Ex.
C-N
N-C

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10
Q

Can beta sheets be formed from peptides parallel to each other instead of antiparallel

A

Yes, the bond would be a bit diagonal to each other

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11
Q

Can there be more than two polypeptides in a beta strand

A

Yes there can be sheets made of multiple strands

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12
Q

What is the side view pattern of a beta stand

What is the length from one down r group to the up r group in the pleated pattern

What about distance between two r groups on the same side?

A

Pleated (zig zag), and the r groups are of alternating side of the sheet (down, up, down , up)

3.5 (opposite)

7 (same)

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13
Q

What is a mixed beta sheet

Give an example of how we’d describe one

A

Mixed sheet are sheets that have antiparallel and parallel strands in the same sheet

Ex. Three strands top 2 para bottom 2 antiparallel

It’s a three stranded mixed beta sheet

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14
Q

One the arrow representation of the beta strands how would they be described

A

They have the arrow pointing to the C terminus

They aren’t flat, they’re usually twisted

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15
Q

What is a reverse turn

A

The third type of secondary protein structure.

This is where the c=o of residue i accepts a h-bond from the nh of residue i+3

This makes the polypeptide change direction and have a turn

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16
Q

What are globular protiens and what does it mean

A

The protiens made by polypeptides have compact globular structures, this means that to get this structure the chain has to switch directions using reverse turns and loops

17
Q

What are loops

A

These help the polypeptide chain change directions

They are exposed to the aqueous environment and have aa residues that have polar/charged side chains, they’re the primary protiens structure

This means the r groups in loops h bind with water and are hydrophilic

18
Q

What is an example of a fibrous protein with alpha helices

A

Alpha keratin

This is two alpha helices that are wrapped around each other (intertwined) due to weak interactions like can see walls or ionic bonds

Can sometimes also be held together by disulphides bonds (need cysteine residues)

19
Q

What are the characteristics of the fibrous protien collagen

A

Is made up of 3 polypeptide chains

Each chain is made of gly pro pro gly pro pro (GPPGPP)

The 5 memberd rings of the proline stick out and the glycines come close together because they only have H as their side chain.

nh and COO do h bonding to hold them together