Lecture 13 Flashcards

1
Q

What is the Secondary Structures of Proteins?

A

The local folding of the polypeptide backbone

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2
Q

What does the Secondary Structure of polypeptides allow for?

A

Hydrogen bonding of the group in the polypeptide backbone (N-H and C=O)

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3
Q

When do Regular Secondary structures occur?

A

When every amino acid in a segment of the polypeptide adopts the same geometry

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4
Q

What are the two regular patterns of secondary structure?

A

Alpha-helix

Beta-sheets

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5
Q

What are the two important consideration when looking at the structures that polypeptide chains might adopt?

A
  • Minimize steric conflicts

* Maximize hydrogen bonds

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6
Q

Does secondary structure break bonds or form bonds?

A

No, it is just rotating bonds

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7
Q

What do both the alpha-helix and the beta-sheets satisfy?

A

The hydrogen bonding potential and the steric restraints

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8
Q

What are the H-bonds like in Alpha-helices?

A

The carbonyl oxygen of each residue forms an H-bond with the backbone - NH group four residues downstream

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9
Q

What is an Alpha helix?

A

A portion of a polypeptide that forms a right handed helical structure

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10
Q

Which amino acid residues do not form hydrogen bonds in the alpha helix structure?

A

Those at the ends of the backbone

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11
Q

What is the helix axis?

A

The axis that all the hydrogen bonds in a alpha helix is parallel to

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12
Q

What is the proximity of side chains to each other in the alpha helix?

A

The side chains are close to each other in alpha helices

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13
Q

What is the core of an alpha helix entirely made up of?

A

The backbone

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14
Q

What is the arrangement of the amino acid side chains in the alpha helix?

A

They are projecting away from the helix core

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15
Q

How does the orientation of the side chains of amino acids change when going from the primary structure to the alpha helix secondary structure?

A

The amino acid side chains that are 3-4 chains apart from each other in the primary structure become a lot closer in the secondary structure

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16
Q

What are the different ways the projecting side chains in alpha helices can interact favorably?

A
  • Positive and negative charges
  • H bond donors and acceptors
  • Hydrophobic groups near each other
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17
Q

What are the different ways the projecting side chains in alpha helices can interact unfavorably?

A
  • Multiple negative or positive charges as part of their amino acid side chains
  • Too many bulky side chains
18
Q

What can unfavorable interactions between projecting side chains in alpha helices do?

A

They destabilize the structure

19
Q

What is the function of the major groove in B-form DNA?

A

It is the appropriate size to interact and bind to proteins (specifically an alpha helices)

20
Q

What is the similarity between the alpha helix and the major groove of B-form DNA?

A

They are the same diameter

21
Q

What is proline not common in the middle of a double helix?

A

Because the nitrogen is bonded to three carbons and is missing an H to form hydrogen bond interactions and proline is big

22
Q

What is the consequence of a proline being in the middle of an alpha helix?

A

It will cause a kink in the bonds

23
Q

Where is Prolin usually found in an alpha helix?

A

At the end terminal of an alpha helix so it doesn’t have to participate in H-bonds

24
Q

What are Beta-Sheets

A

Multiple beta strands arranged side by side and strands are joined by loops or other structures

25
What are the two types of Beta-sheets?
Parallel and antiparallel sheets
26
What occurs in parallel beta sheets?
All the strands go from N to C or from C to N
27
What occurs in anti parallel beta sheets?
The strands alternate going from N to C and C to N
28
What kind of hydrogen bonding interactions are seen in Parallel Beta sheets?
Alternating angled hydrogen bonds making wedged shapes
29
What are the H bond interactions between antiparallel beta sheets?
The hydrogen bonding pattern occurs in parallel couplets
30
What is the arrangement of the amino acids in beta-sheets?
The individual amino acid side chains alternate above and below the plane of the beta-sheet
31
Which amino acid side chains are found next to each other in beta sheets?
Every second amino acid is found next to the other amino acids that are either two before or two after it. Every second side chain is interacting
32
What forces stabilize alpha-helices and beta-sheets?
H-bonds between backbone CO and NH groups in the same helices
33
Where do H-bonds within beta sheets come from?
Interactions between the individual strands
34
What are the regular secondary structures?
Alpha helices and beta sheets
35
What is meant by regular secondary structures?
The peptide backbone has the same configuration/conformation for every amino acid within the secondary structure
36
What are distinct elements of regular secondary structures linked together by?
Polypeptide loops of various sizes
37
What bond does a rotation required for alpha helices and beta sheets occur at?
All the bonds but the peptide bond (C-N)
38
Why is the statement both alpha helices and beta sheets form from only consecutive amino acid residues in a polypeptide false?
Because beta sheets have to come from different portions of the primary structure
39
What is Tertiary structure concerned with?
All the atoms in the structure, backbone, sidechain and in some cases the prosthetic groups
40
What are the two types of tertiary structure?
* Fibrous (elongated) | * Globular (compact)
41
What are the characteristics of Fibrous proteins?
* Insoluble in aqueous solutions * Form long protein filaments * Usually structural or connective properties
42
What are the characteristics of Globular proteins?
* Soluble in aqueous solution | * Fold into compact structures with nonpolar cores and polar surfaces