protein structure Flashcards

1
Q

What are proteins?

A

Proteins are linear polymers of amino acids joined
by peptide bonds.

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2
Q

What is the smallest protein length? What is the average protein length? What is the largest known protein?

A

The smallest proteins are ~40 amino acids in
length. The “average” protein is ~300-400 amino acids in
length. The largest known protein is the muscle protein titin: ~30,000 amino acids!

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3
Q

What is the specific sequence of amino acids in a
protein called?

A

The specific sequence of amino acids in a protein is
called the protein’s primary structure.

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4
Q

Do linear polymers of amino acids form straight
rod-like structures?

A

No, but fold into definite 3-D structures
depending on the sequence of amino acids.

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5
Q

What determines the functions of a protein?

A

The functions of a protein are determined by :
-its overall shape (i.e., specific folding pattern driven by amino acid sequence)
-the distribution throughout that overall shape of the amino acid side chains with their distinctive chemical properties.

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6
Q

What are the two major classes of amino acid side
chains?

A

Hydrophilic and Hydrophobic.

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7
Q

What is the charge distribution of hydrophilic side
chains?

A

They have a polar electronic charge distribution.

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8
Q

What is the charge distribution of hydrophobic side
chains?

A

They have a non-polar charge distribution.

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9
Q

What is the hydrophobic effect?

A

Water molecules surrounding hydrophobic molecules dispersed in water
adopt a constrained, cage-like organization (low entropy).
If hydrophobic molecules coalesce, constrained water molecules is reduced, and this net increase in entropy
ultimately drives the formation of separate hydrophobic and aqueous phases.

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10
Q

What type of interactions favor the coalescence of
hydrophobic molecules?

A

Weak non-covalent van der Waals intermolecular
interactions.

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11
Q

What is the “Oil drop” model of protein folding?

A

It is a model that takes into account the hydrophobic
and hydrophilic side chains of amino acids and their
interactions in an aqueous solution.

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12
Q

What determines the overall shape of the molecule?

A

specific, local, structural interactions, called secondary
and tertiary, determine the path of the peptide “backbone”
through space and hence, the overall shape of the molecule.

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13
Q

What dictates protein structure and function?

A

The amino acid sequence

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14
Q

What is the relationship between DNA and protein
function?

A

DNA indirectly determines protein function through
its determination of the amino acid sequence.

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15
Q

How do amino acids link together? (Process)

A

The amino acids of a polypeptide are attached to their neighbors by covalent bonds known as a peptide bonds. Each bond forms in a dehydration synthesis (condensation) reaction. The carboxyl group of the amino acid chain reacts with the amino group of an incoming amino acid, releasing a molecule of water. The resulting bond between amino acids is a peptide bond

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16
Q

What is the directionality of amino acids in a protein
chain?

A

it has two ends that are chemically distinct from one another. At one end, the polypeptide has a amino group, and this end is called the amino terminus (or N-terminus). The other end, which has a carboxyl group, is known as the carboxyl terminus (or C-terminus).

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17
Q

What is the secondary structure of polypeptides?

A

local conformations of the
peptide chain backbone.

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18
Q

What are the two major peptide chain backbone
conformations?

A

Alpha-helix and beta-sheet.

19
Q

What is the basis for the alpha-helix and beta-sheet
structures?

A

H-bonding between peptide bond carbonyl O atoms
on one amino acid residue and amino group
hydrogens on a different amino acid residue.

20
Q

What drives the periodicity of the alpha-helix
structure?

A

The tilted axis of H-bonds, which drives a periodicity
of 3.6 monomers per turn. (or 36aa per 10 turns)

21
Q

What determines the surface properties of an
alpha-helix?

A

side-chains

22
Q

What is the gross structure of an alpha-helix?

A

Straight rod.

23
Q

What links two adjacent beta-strands in a
beta-sheet?

A

H-bonds.

24
Q

What determines the interactions of a beta-sheet
with other parts of the protein?

A

Amino acid side chains protruding above and below
the plane of the sheet.

25
Q

Beta-sheet strands can be _________ or ___________.

A

parallel
antiparallel

26
Q

What is the difference between secondary and
tertiary structure?

A

Secondary structure is local, while tertiary structure
is the overall conformation of the polypeptide.

27
Q

What mediates interactions between different parts
of a protein and between the protein and its ligand
GDP?

A

Amino acid side chains.

28
Q

What are the types of non-covalent bonds that drive
interactions among amino acids in a protein? (4)

A

-H-bonds among peptide backbone carbonyl and amino groups
-H-bonds between amino acid side chains with polar side chains
-ionic bonds between positively charged (basic) and negatively charged (acidic) side chains
-van der Waals interactions among hydrophobic side chains.

29
Q

What is the covalent bond interaction that can be
important in protein structure?

A

The side chain of the amino acid cysteine contains
a sulfhydryl group that can form covalent S-S
(disulfide) bonds with other cysteine side chains

30
Q

What are motifs of protein structure?

A

Combinations of secondary structures forming
distinct local 3D structure.

31
Q

What motif is involved in protein:protein interactions?

A

coiled-coil motif

32
Q

What is a Ca++-binding motif?

A

EFhand/helix-loop-helix motif

33
Q

What is a motif that is common in transcription factors: binds to DNA/RNA?

A

Zinc-finger motif

34
Q

What is the difference between a motif and a
domain in protein structure?

A

Motifs are generally small, local structures that do
not contain a sufficient number of structure-maintaining bonds to hold the motif in its
characteristic 3-D shape if it is cut away from the
rest of the protein, while domains are larger than
motifs and contain a sufficient number of bonds to
hold the domain in its characteristic shape if it is cut
away from the rest of the protein.

35
Q

What is a heptad repeat?

A

It is a repeating pattern of amino acids in protein
structure that is commonly represented as
HxxHxxxHxxHxxxH, where H represents a
hydrophobic amino acid and x represents any
amino acid.

36
Q

What is the significance of the rest of the protein in
relation to motifs and domains?

A

The rest of the protein contributes to the stability of
a motif, but contributes little to the stability of a
domain.

37
Q

What are domains in protein structure?

A

Domains are structurally independent entities,
although covalently-joined to the rest of the protein.

38
Q

What are the four major structural classes of protein?

A

-Fibrous protein
-Globular protein
-Integral membrane protein
-Intrinsically disordered protein

39
Q

What is a intrinsically disordered protein?

A

Proteins (or protein segments) that exist as random coils under physiological conditions.
May adopt a specific secondary/tertiary structure upon binding to a well-structured partner protein.

40
Q

True or False: Similar domains cannot be found in diverse proteins, and also as multiple
similar copies within any given protein.

A

False
Similar domains can be found in diverse proteins, and also as multiple
similar copies within any given protein.

41
Q

Domains (HA1 and HA2) are held together by ________ bonds. The three identical two-protein
subunits are held together by ___________ bonds.

A

non-covalent
non-covalent

42
Q

True or False: Multimeric proteins can contain any number of identical or different polypeptides

A

True

43
Q

What are supramolecular complexes?

A

Large “molecular machines” made up of multiple distinct proteins,
each of which may itself contain multiple subunits.
(They are not stable and fall apart when the job is done).

44
Q

True or False: Evolution is to maintain the function of the protein, not the aa sequence.

A

True