Lecture 9: The Structure of Proteins Flashcards

(59 cards)

1
Q

the sequence of amino acids is specified by the __ sequence encoding the protein

A

gene

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2
Q

amino acid polymers of less than 50 amino acids are called __

A

peptide

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3
Q

a peptide bond is formed between which two groups in a peptide chain?

A

carboxyl group of the first and the amino group of the second

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4
Q

the H and R groups are opposite the ___ in a peptide bond to avoid steric clash

A

o in the carbonyl

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5
Q

the equilibrium of making a peptide bond favours the ___ side

A

left (hydrolysis)

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6
Q

why does the peptide equilibrium favour the hydrolysis rather than synthesis?

A

because the synthesis requires free energy

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7
Q

the alpha carbon can always be identified because it has the ___ attached to it

A

R group

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8
Q

each amino acid in a peptide chain is called a __

A

residue

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9
Q

every peptide chain begins with a ___ residue and ends in a __ residue

A

amino, carboxyl

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10
Q

the amino acid at the beginning of the chain is called the __

A

amino / N terminus

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11
Q

the amino acid at the end of the chain is called the __-

A

carboxly / C terminus

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12
Q

the geometry of an aa about a peptide bond is __

A

planar

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13
Q

what makes the peptide bond rigid? (not free to rotate)

A

resonance from the carboxyl makes the bond not purely single and therefore unable to freely rotate

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14
Q

the psi and phi bonds flank the ___ of each amino acid

A

alpha carbon

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15
Q

what bonds are free to rotate in amino acids?

A

the phi and psi bonds

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16
Q

the phi bond forms between the alpha carbon and the

A

amino group

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17
Q

the psi bond forms between the alpha carbon and the

A

carbonyl group

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18
Q

what does a Ramachandron plot show?

A

the permissible phi and psi bond angles allowed in a polypeptide backbone

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19
Q

the range of permissible angle combinations reflect the ___ and ___structure of proteins

A

secondary and tertiary

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20
Q

the polypeptide structure will have inherent __ and ___ within the constraints dictated by the permissible angles

A

flexibility and mobility

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21
Q

the secondary structure of proteins is stabilized by __ bonds between N and carboxyl groups in linear squence

A

H bonds

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22
Q

due to combination of bond angles and H bonding effects, certain aa segments ____ form secondary structures

A

spontaneously

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23
Q

what are the 3 types of secondary structures?

A

aplha helix , beta sheets, turns and loops

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24
Q

proteins can be made exclusively of alpha helix/beta sheets, or a mix of both (T/F)

25
turns and loops function to __
connect helices or sheets together
26
alpha helixes are segments of amino acids that form ___ handed helical structure (rotates ___ (cw.ccw)
right; clockwise
27
what is the average length of an alpha helix?
10 amino acids
28
there are about ___ amino acids per complete turn along the the alpha helix
3.6
29
in the alpha helix, every ___ amino acid interacts via hydrogen bonding
4
30
side chains extend in what direction with respect to the helix?
outwards
31
what makes some amino acids unsuited for helix formation?
geometry or size of side chains
32
about ___ % of all soluble proteins are composed of alpha helices
25
33
the B sheets are made by multiple __ of amino acids in a ___ sequence rather than coiled in a helix
adjacent segments; fully extended
34
adjacent segments in a B sheet interact by __ interactions
hydrogen bonding
35
adjacent B strands can be in anti-parallel or parallel (T/F)
true
36
in antiparallel B sheets, each amino acid is bonded to __ on the other strand
one amino acid
37
in parallel B sheets, each amino acid is bonded to __ on the other strand
2 different amino acids
38
in parallel B sheets, the two strands run in the ___ direction
same
39
in antiparallel b sheets, the two strands run in the ___ direction
opposite
40
B strands associate to become __
B sheets
41
B sheets are stabilized by intracellular ___ bonds
H
42
arrows representing B sheets point in the direction of the ___ terminal end
carboxyl
43
Beta sheets can be flat, but most adopt a ___ shape
twisted
44
what two amino acids participate in forming turns?
proline and glycine
45
there is open space in the interior of a protein (T/F)
no; little to none
46
name 5 things that stabilize tertiary structure
1. charge interactions 2. H bonding 3. van der waal between side chains 4. hydrophobic effect 5. disulphide bonds b tween cysteine side chains
47
myoglobin is an example of a __ protein
globular
48
myoglobin is an extremely compact molecule made of __ polypeptide chain(s) of ___ (#) amino acids
1; 153
49
about 70% of the myoglobin structure is made of __
alpha helices
50
tertiary structures of many proteins can be divided into __ and ___ units
structural and functional
51
some proteins fold into multiple tertiary structures called __
domains
52
each domain may posses a unique ___ that may be quite functional even id separated from the protein
enzymatic function
53
discrete sub-structures in a protein with special structural/functional significance are called __
motifs
54
what motif is typically found in proteins that bind double-stranded DNA?
helix--turn--helix
55
each polypeptide chain in a protein complex is called a __
subunit
56
quaternary structure refers to the arrangement of ___ and the nature of their interactions
subunits
57
what is homotypic association?
proteins assemble within each other
58
what is heterotypic association?
different proteins assemble into multi-subunit complexes
59
example of a heterotypic protein
DNA polymerase