Chapter 5- Secondary Structure Flashcards

1
Q

Primary structure definition

A

amino acid sequence of protein

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2
Q

Secondary structure definition

A

local spatial arrangements of the backbone atoms

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3
Q

Tertiary structure definition

A

3D structure of the entire polypeptide chain

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4
Q

Quaternary structure definition

A

Spatial arrangements of protein subunits

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5
Q

Peptide bonds are ____ bonds

A

amide bonds

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6
Q

Proteins result from the formation of covalent peptide bonds by

A

Condensation

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7
Q

A polymer of two amino acids is called

A

dipeptide

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8
Q

A polymer of many amino acids

A

polypeptide

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9
Q

Avg mass of amino acid

A

110 g/mol

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10
Q

Polypeptides are _____ polymers not branched

A

linear

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11
Q

The alpha H bonds and carboxyl groups run in the _____ direction

A

same

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12
Q

Amino acids are always read from the __ terminus to the __ terminus

A

N (amino terminus), C

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13
Q

In a peptide group a C–N bond is ___ than a simple amine, while a C=O bond is ____ than a simple ketone

A

Shorter, Longer

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14
Q

Peptide bond has _____ double bond character

A

~40%

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15
Q

C–N torsion angle is called __ and the C–C torsion angle is called ___

A

Phi, Psi

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15
Q

The trans configuration is more favored than the cis configuration because

A

the trans configuration has less steric hindrance and is more stable

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15
Q

the C–N bond is unable to ____

A

Rotate

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15
Q

Side chains dictate the bond angles because

A

different bond angles reorient to accommodate other groups around it

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16
Q

An alpha helix can be right-handed or left-handed which means it has

A

Chirality

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16
Q

Glycine in a peptide chain provides

A
  • flexibility to proteins
  • often found in places where proteins make sharp turns
16
Q

Proline in a protein chain provides

A
  • structure rigidity (due to cyclic side chain)
  • may be found in kinks of the protein
17
Q

polypeptide made of L-alpha amino acids will have n=___ and pitch =____

A

3.6 amino acids per turn, 5.4 A

18
Q

____ and _____ of peptide bond point along the long axis (in the opposite direction)

A

N-H, C=O

19
Q

The sum of all H bonds contributes to stability which means

A

more H bonds= more stability

20
Q

side chains in an alpha helix point

A

outwards (avoids steric interference)

21
Q

How do side chains affect stability?

A
  1. affecting the peptide backbone
  2. through side chain- side chain interactions
22
Q

How many degrees between each amino acid in an alpha helix

A

100

23
Q

interactions between side chains can lead to either the ______ or _______ of the helix

A

destabilization or stabilization

24
Q

Steric clash means

A

two large bulky side chains stacked on top of each other is more likely to destabilize the helix

25
Q

ASP and LYS have formed a _____ interaction

A

salt bridge that stabilizes the helix (different charges)

26
Q

Asp and Glu have a _____ interaction

A

repulsion interaction that destabilizes the helix (same charges)

27
Q

Aromatic amino acids can ____ which are favorable ______ ________

A

stack ( pi stacking), hydrophobic interactions

28
Q

amino acids that tend to form an alpha helix

A

MALEK (met, ala, leu, glu, and lys)

29
Q

Beta-branched amino acids that make them more difficult to adopt an alpha-helical conformation

A

Val, Ile, Thr

30
Q

Amino acid that is entropically expensive and destabilizes helices

A

Gly

31
Q

Conformationally rigid with no H bonding possible, known to destabilize helicies and may form a kink

A

pro

32
Q

All dipoles in an alpha helix point in the ____ direction which results in a ______ ______ between the C terminal and N terminal

A

same, macro dipole (c end is neg and N end is pos)

33
Q

Dipoles in an alpha helix result in

A

destabilization through entropic effects

34
Q

the N terminal of an alpha helix is often capped by a _____ side chain while a ____ side chain caps a C terminal

A

negative, positive

35
Q

Antiparallel beta sheets involve two chains running in ____ directions, the H bonds are ~ ______ to each other

A

opposite, parallel

36
Q

Parallel beta-sheets involve two side chains running in the _____ directions, the H bonds are formed on ____

A

same, angles

37
Q

Beta strands exhibit a _____ ______ ______ due to the chirality of the amino acids

A

right-handed twist

38
Q

Beta turns are commonly formed by

A

proline and glycine

39
Q

beta turns give proteins _____ and promotes the formation of _______ ______ ____

A

globularity, anti-parallel beta sheets

40
Q

The coil/loop conformation is completely ______ and is typically found on the _____ _____ of the proteins

A

unstructured, outer surface

41
Q

Random coils are usually ______ and ______ but do not conform to any ______ ______ ____

A

organized and stable, frequently recurring pattern

42
Q

The stability of seconds structures is determined by

A
  1. steric repulsion minimized
  2. H bonding is maximized
43
Q

Characteristics of Circular Dichroism Spectroscopy

A
  • absorption spectroscopy
  • provides information on the secondary structure content of proteins
  • signal; originated from the amide group and the phi/ psi angles