Ch. 6 Flashcards

(64 cards)

1
Q

Angle between Nitrogen and alpha Carbon

A

Phi (Φ)

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2
Q

Angle between alpha carbon and carbonyl carbon

A

Psi (Ψ)

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3
Q

What is the shaded area of a Ramachandran plot

A

most favorable Φ and Ψ angles

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4
Q

What are the 3 secondary structures

A

α-helix, β-sheets, and turns and cross overs

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5
Q

How are α-helices stabilized

A

Backbone stabilized by H-bonds spaced 4 residues apart

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6
Q

Residues per turn in an α-helix

A

3.6

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7
Q

Most common orientation of α-helices in nature

A

right handed (Φ=-60, Ψ=-50)

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8
Q

What effect do side chains have in an α-helix

A

Determines solubility in water

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9
Q

What amino acids can be considered helix breakers

A

Proline and Glycine

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10
Q

How are β-sheets stabilized

A

Backbone is stabilized by H-bonding between separate β-strands

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11
Q

What are β-strands composed of

A

tight α-helix with 2 residues per turn

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12
Q

Orientation of R groups in β-strands

A

180 apart

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13
Q

3 types of β-sheets

A

parallel (N-terminals start at same sport), anti-parallel, and mixed (both parallel and anti-parallel)

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14
Q

3 ways to change direction

A

Proline, β-turn, and cross over

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15
Q

What conformation around the peptide bond allows proline to have a natural turn

A

cis conformation

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16
Q

How to form β-turn

A

H-bond between carbonyl oxygen of a residue with the amide proton of another residue 3 AA away

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17
Q

Favored AAs in β-turns

A

Glycine (less sterics) and Proline (natural curve)

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18
Q

What is a cross over

A

short α-helical segment that connects β-strands

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19
Q

Two types of Fibrous proteins

A

keratin (hair and nails) and collagen (skin, bones, tendons, blood vessels)

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20
Q

Structure of the initial monomer in keratin

A

central right handed α-helix (rod domain)

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21
Q

two initial keratin monomers form a dimer called

A

left handed coiled coil

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22
Q

Why do coiled coils form

A

red domain is composed of heptad repeats that create a non-polar strip on the outside of the helix (hydrophobic effect)

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23
Q

Two coiled coils associate to form?

A

protofilament

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24
Q

Two protofilaments associate to from?

A

right handed protofibril

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25
4 protofibrils form?
keratin filament
26
Why do protofilaments and protfibrils form
H-bonding or disulfide bonds
27
Structural difference between hair and nails
relative amounts of H-bonds (flexible) and disulfide bonds (rigid)
28
Structure of initial collagen monomer
left handed α-helix with 3.3 residues per turn
29
AA composition of collagen
High in Glycine and Proline
30
What amino acids are formed after the protein is formed
4-hydroxy proline, 3-hydroxy proline, and 5-hydroxy lysine
31
Enzyme that forms hydroxy proline
prolyl hydroxylase
32
Enzyme that forms hydroxy lysine
lysyl hyroxylase
33
Effect of hydroxylating proline and lysine
increases H-bonding
34
Key molecule in formation of hydroxy proline
Vitamin C
35
3 collagen monomers associate to form?
right handed triple helix (tropocollagen)
36
AA pattern found in collagen
Gly-X-Y X=proline Y=hydroxyproline
37
Location of glycine in tropocollagen
buried in interior b/c of glycines low sterics
38
What holds tropocollagen together
H-bonding in the hydroxy proline backbone
39
tropocollagen forms?
collagen fibers
40
What holds collagen fibers together
covalent crosslinks
41
Lysine can be oxidized to what
aldehyde form (allysine)
42
Lysine and allysine crosslink?
imine (schiff base)
43
allysine and allysine crosslink?
aldol condensation
44
Disrupting cross links does what to collagen
destabilizes collagen
45
Why does a vitamin C deficiency (scurvy) cause a diseased state
Hydroxy proline can not be made without vitamin C, disrupting the structure of collagen
46
Tertiary structures form the most stable structure through?
covalent and non-covalent interactions
47
Globular protein themes
α-helices and β-sheets in core cavities filled with hydrophobic side chains water stabilized the surface
48
What are protein domains
distinct tertiary regions connected by a flexible backbone
49
Levinthals paradox in relation to protein folding
protein folding is not random
50
What does mean that protein folding is all or nothing
remains folded until Tm then rapidly unfolds
51
Folding themes
1. secondary structures fold first 2. hydrophobic collapse 3. long-range interactions
52
Intermediate folded shape?
molten globules
53
what does it mean that proteins are marginally stable
they have flexibility and motion
54
Why is protein folding represented as a funnel
each step leads to an intermediate lower in energy making each step easier than the last
55
What are molecular chaperones
proteins that help other proteins fold
56
Example of molecular chaperone
heat shock proteins (HSP-90)
57
Effects of Misfolding
loss of function and can lead to aggregation
58
Examples of misfolding
sickle cell, alzheimers, and cancer
59
What is an IUP
intrinsically unstructured protein
60
What AAs are found in IUPs
polar AAs and proline
61
Function of IUPs
can bind ligands and can increase surface area
62
Advantages of quaternary structure
Stability Genetic economy Bring catalytic sites together Cooperativity
63
Example of Cooperativity in quaternary structures
ligand binding at one subunit can trigger a conformational change in another
64
What is Allostery
information transfer across long distances in a protein