exam 2 protein shape and structure Flashcards

1
Q

what is protein structure determined by

A

the sequence of amino acids

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2
Q

what can proteins be divided into

A

functional and structural domains

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3
Q

what are function and structural domains

A

independently folding subregions within the protein sequence

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4
Q

what determines a protein’s function

A

the 3D structure of it

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5
Q

what is primary structure of proteins

A

linear sequence of amino acid residues determined by the mRNA code

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6
Q

what is primary structure held together by

A

peptide bonds between amino acids

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7
Q

what determines higher order structures

A

protein structure in combination with a protein’s environment

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8
Q

what is the sequence of proteins different from

A

the sequence that initiates folding process

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9
Q

what is the secondary structure of a protein

A

the folding and twisting of peptide backbone

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10
Q

what is the secondary structure held together by

A

weak H-bonds between C=O (carbonyl) and N-H (amine) groups in the backbone

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11
Q

what do the two bonds of every amino acid have

A

the two bonds have freedom of rotation

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12
Q

what is the purpose of side chains in the secondary structure

A

they make it more or less difficult for structure to form, but don’t hold secondary structure together

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13
Q

what are the two secondary structures

A

alpha helices and beta sheets

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14
Q

what is the structure of the alpha helix

A

rigid cylindrical structure

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15
Q

when does an alpha helix form

A

forms when H-bonding occurs between a carbonyl and amine group that are 4 amino acids apart on the polypeptide backbone

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16
Q

what makes one turn of the helix

A

four amino acids

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17
Q

what direction does coiling of the alpha helix happen in

A

a clockwise direction down the length of the chain

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18
Q

what is the beta sheet

A

a flat, folded, sheet-like structure

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19
Q

when does a beta sheet form

A

when H-bonding occurs between a carbonyl and amine group on adjacent polypeptide chains

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20
Q

what does it mean for an adjacent beta sheet chain to be parallel

A

adjacent chains run N-terminal to C-terminal

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21
Q

what does it mean for an adjacent beta sheet chain to be antiparallel

A

adjacent chains run in opposite directions

22
Q

what do rigid proline residues do

A

insert a kink in a protein’s backbone and disrupt secondary structures

23
Q

what is tertiary structure of proteins

A

3D arrangement of secondary structures to assume the lowest possible energy state

24
Q

what is tertiary structure (detailed)

A

stretches of proteins that serve as links between secondary structures to allow them to fold up

25
Q

what is tertiary structure held together by

A

non-covalent attractions between R-groups along with R-groups + the surrounding environment

26
Q

what links secondary structures together to form tertiary structures

A

unstructured loops (aka random coils)

27
Q

what can tertiary structure stabilized by

A

covalent interactions - most important are disulfide bonds

28
Q

where can covalent disulfide bonds form to stabilize tertiary structures

A

between cysteine residues to cross-link parts of the polypeptide backbones

29
Q

what does stabilizing tertiary structures do

A

makes it more difficult to unfold once it’s in the shape

30
Q

what is the difference is the energy of unfolded and folded proteins

A

unfolded proteins have a higher free energy than when it’s folded due to entropy

31
Q

what does protein stability depend on

A

the free energy change between the folded and unfolded states

32
Q

what is delta G

A

G(folded) - G(unfolded) : products minus reactants

33
Q

what charge creates the most stable folded protein

A

the most negative the change in free energy

34
Q

what are molecular chaperones (chaperonins)

A

provide an isolated chemical environment in which they can fold, which proteins require to 3D fold

35
Q

what is a prion

A

an infectious protein

36
Q

what are prions evidence of

A

that some unusual contagious neurological diseases are caused by proteins alone

37
Q

what happens when a prion protein interacts with a correctly folded protein

A

it recruits it to also fold incorrectly (ex: mad cow, kuru)

38
Q

what is a protein domain

A

a region of the protein that folds essentially independently of other regions

39
Q

how many protein domains can a protein have

A

single or multiple

40
Q

what does a domain represent

A

a functional region of the protein - different domains have different function

41
Q

what do catalytic protein domains do

A

inhibit host cell protein synthesis

42
Q

what do hydrophobic protein domains do

A

inserts into the membrane

43
Q

what do receptor binding protein domains do

A

attach to cell surface

44
Q

what are motifs

A

similar domains that occur in many related proteins

45
Q

what is quaternary protein structure

A

arrangement of multiple tertiary structures

46
Q

what are quaternary structures held together by

A

weak bonds and some disulphide bonds

47
Q

what are homomers of quaternary structures

A

identical subunit polypeptides

48
Q

what are heteromers of quaternary structures

A

different subunit polypeptides

49
Q

what is the final structure of a protein after quaternary structure

A

mature protein

50
Q

what does a higher order structure increase

A

efficiency