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biochem > (M) Peptides and Proteins part 2 (ppt and lec based) > Flashcards

(M) Peptides and Proteins part 2 (ppt and lec based) Flashcards

1
Q

enumerate the levels of protein structures

A

primary (1°)
Secondary (2°)
Tertiary (3°)
Quaternary (4°)

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2
Q

this is the linear sequence of amino acids, primary structure of insulin

A

primary

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3
Q

this is the simplest level of complexity describing the structure of protein

A

primary

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4
Q

the primary protein structure refers to

A

quantitative aa composition

sequence of aa

number of peptide chains

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5
Q

how many dipeptides are possible from 20 protein derived aa?

A

There are 20 x 20 = 400 dipeptides possible

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6
Q

how many tripeptides are possible from the 20 protein derived aa?

A

There are 20 x 20 x 20 = 8000 tripeptides possible

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7
Q

T or F
the number of peptides possible fo a chain of n amino acid is 20xN

A

F (20^n)

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8
Q

T or F
the most abundant amino acid proteins are Trp, Cys, Met, and His

A

F (rarest)

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9
Q

T or F
The most abundant amino acid in proteins are Leu, Ala, Gly, Ser, Val, Met and Glu

A

F (remove Met)

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10
Q

protein structure created by the formation of hydrogen bonds between peptide bonds

A

secondary protein structure

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11
Q

who proposed the two secondary structures in proteins

A

Pauling and Corey

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12
Q

two types of secondary structures

A

alpha-helix
beta-sheet

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13
Q

types of secondary structures of protein:

Rod-like structure (phonecord)

A

alpha-helix

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14
Q

T or F in alpha helix, aa R groups extend inward from the helix

A

F (outward)

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15
Q

T or F

main chain atoms are outside

A

F inside

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16
Q

T or F
Helices can be right or left-handed

A

T

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17
Q

how is the carbonyl of each amino acid in alpha helix bonded to the amide

A

H-bonded

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18
Q

Why does proline destabilize alpha helices

A

its rigid ring prevents the n-c bond from rotating

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19
Q

Why is it important that the n-c bond rotate?

A

so that an amide group will b able to form intrachain hydrogen bonds

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20
Q

example of bulky r groups that destabilize alpha helices

A

val, ile, leu, pro, met (branched amino acids)

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21
Q

T or F

presence of parallel similarly charged amnio acids destabilize alpha helices

A

F (adjacent)

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22
Q

Second most commonly occurring protein 2° structure

A

beta pleated sheet

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23
Q

formed when 2 or more polypeptide chains are linear and stacked at top of each other

A

beta pleated sheet

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24
Q

where does r groups lie within the pleated sheet

A

above or below the zigzagging planes

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25
Q

in what orientation does the r group lie in relation to the pleated sheet

A

perpendicular to the pleated sheet

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26
Q

how is the carbonyl of each amino acid in beta pleated sheet bonded to the amide

A

H-bonded (parehas lang sila akshwally sa alpha helix)

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27
Q

two types of beta pleated sheet

A

antiparallel and parallel

28
Q

T or F
parallel beta pleated sheets are more stable than the antiparallel

A

F (less stable)

29
Q

this type of beta pleated sheet is composed of :

one strand of NH and carbonyl group, h-bonded to carbonyl group and N-H group of the opposing amino acid on the other strand

A

Anti-parallel beta sheet

30
Q

5 ways that tertiary structures are stabilized

A

covalent bonds
hydrogen bonds
salt bridges
hydrophobic interactions
metal ion coordination

31
Q

5 ways that tertiary structures are stabilized:

this stabilizes the native conformation of the protein

A

covalent bonds

32
Q

5 ways that tertiary structures are stabilized:

these are bonds in the interior of the protein

A

hydrogen bonding

33
Q

5 ways that tertiary structures are stabilized:

attracts the NH3+ group and the -COO- group

A

salt bridges

34
Q

5 ways that tertiary structures are stabilized:

these are interaction between nonpolar side chains

A

hydrophobic interaction

35
Q

5 ways that tertiary structures are stabilized:

major force stabilizing tertiary structure

A

hydrophobic interaction

36
Q

5 ways that tertiary structures are stabilized:

linkage via metal ion

A

metal ion coordination

37
Q

if you see this card, familiarize yourself with the tertiary protein structure visual aid

A

thanks mwah galingan mo bading

38
Q

This is the highest level of protein organization

A

quaternary (4°) protein structure

39
Q

in which proteins are quaternary structures found?

A

in proteins that have 2 or more polypeptide chains (subunits)

40
Q

escribes the characteristic manner in which the individual , folded polypeptide chains fit each other or interact with one another so that they can act as one single molecule

A

quaternary structure

41
Q

how are the chains held together in a quaternary structure

A

hydrogen bonds
salt bridges
hydrophobic interactions

42
Q

quaternary levels:

has 2 polypeptide chains / subunits

A

dimer

43
Q

quaternary levels:

3 polypeptide chains / subunits

A

trimer

44
Q

quaternary levels:

has 4 polypeptide chains / subunits

A

tetramers

45
Q

quaternary levels:

has 5 polypeptide chains / subunits

A

pentamer

46
Q

Process by which a protein structure assumes its functional shape or conformation

A

Protein Folding

47
Q

process in which a protein chain acquire its 3-dimensional structure from a random coil

A

Protein Folding

48
Q

what is the native state of the protein

A

folded protein

49
Q

what assists proteins in folding and prevents it from associating with inappropriate molecules

A

chaperones

50
Q

example of chaperone protein discovered from E.coli bacterium

A

-hsp 70

51
Q

T or F

Allergies develops from failure of protein to fold into a native structure

A

T

52
Q

T or F

Failure of proteins to fold can cause improved memore

A

F (can lead to Parkinson’s and Alzheimer’s)

53
Q

T or F

The protein will be more active if it failed to fold properly to compensate

A

F (inactive)

54
Q

The process of destroying the native conformation of a protein by chemical or physical means

A

denaturation

55
Q

denaturing agent:

disrupts hydrogen bonding

A

heat and 6M Aqueous urea

56
Q

denaturing agent for hydrophobic regions

A

detergents

57
Q

denaturing agent for salt bridges and h bonds

A

acids and bases

58
Q

denaturing agent for disulfide bonds

A

reducing agents and heavy metal ions

59
Q

basic amino acids with an overall positive charge

A

lys, arg, and his

60
Q

acidic amino acids with overall negative charge

A

glu, asp

61
Q

T or F

Proteins to be insoluble should be able to interact as much as possible with the solvent

A

F (should be soluble)

62
Q

what is the charge of proteins at the isoelectric point

A

net zero charge

63
Q

what is the net charge of protein above pI

A

negative

64
Q

what is the net charge of protein below pI

A

positive

65
Q
A

biochem (31 decks)

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