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Biochemistry Fall MS1 > Amino Acids and Proteins > Flashcards

Amino Acids and Proteins Flashcards

1
Q

structural or mechanical roles, polypeptides are intertwined to form cables or fibers

A

fibrous proeins

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2
Q

are functional or nonstructural, chains folded on itself to give compact rounded structure and are water soluble

A

globular proteins

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3
Q

aspartate is

A

acidic amino acid

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4
Q

glutamate is

A

acidic amino acid

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5
Q

arginine

A

basic

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6
Q

lysine

A

basic

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7
Q

histidine

A

basic

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8
Q

nonpolar

A

glycine, alanine, leucine and phenylalanine

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9
Q

serine, cysteine, threonine and tyrosine

A

neutral

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10
Q

glycine, alanine, leucine and phenylalanine

A

nonpolar

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11
Q

what forms of amino acid are found in humans

A

L forms

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12
Q

sulfur containing amino acids

A

methioine and cysteine

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13
Q

aromatic compounds

A

phenylalanine, tyrosine, and tryptophan

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14
Q

nonpolar

A

glycine, alanine, proline, valine, leucine, and isoleucine

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15
Q

polar

A

asparagine, glutamine, serine and threonine

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16
Q

2 cysteins can spontaneously oxidize to produce

A

cystine via a disulfide bridge

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17
Q

__________is a genetic disease resulting in defective transport protein that reabsorbs cystine into renal tubular cells and apppears in urine and forms calculi

A

cystinuria

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18
Q

_______is the sequence of amino acids in a polypeptide chain

A

primary structure

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19
Q

peptide bond is

A

carboxyl end and amino acid

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20
Q

__________is the folding or coiling of the chain to give regular repeated motifs

A

secondary structure

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21
Q

intramolecular H-bonding

A

between different parts of the same chain

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22
Q

intermolecular H bondingq

A

between different chains

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23
Q

how are secondary structures stabilized

A

stabilized by hydrogen bonds formed between the carbonyl oxygen of one peptide bond and the amino hydrogen of another

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24
Q

intermoleclar hydrogen bonding and intramolecular hydrogen bonding

A

beta pleated sheet

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25
Q

intramolecular hydrogen bonding

A

alpha helix

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26
Q

____________secondary structures is strong, non-elastic and flexible

A

beta pleated sheat

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27
Q

strong and may be elastic type of secondary structure

A

alpha helix

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28
Q

_______are strong rope like strucutres of intertwised alpha helices which are a major component of external protective layers in mammals

A

keratins

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29
Q

_______have high sulfur content and many S-S bonds

A

hard keratins

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30
Q

_______have low sulfur content and few S-S bonds between the chains

A

soft keratins

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31
Q

___________are a family of extracellular glycoproteins and are a major protein of connective tissue and forms insolbule fibers of great strength

A

collagnes

32
Q

composition of collagens

A

rigid, cross linked triple helical rods

33
Q

collagen has a high content of

A

glycine, proline, hydroxyproline and lysine

34
Q

what two amino acids confer collagens rigidity

A

pro and hyp

35
Q

what is the fundamental unit of collagen

A

tropocollagen

36
Q

____________is a triple helical rod that is rigid and has a wider pitch than alpha helix to accomodate the bulky pro and hyp residues

A

collagen

37
Q

________-is the modification of a structure after synthesis of the poypeptide chain

A

post-translational modification

38
Q

_______ and ________ residues are hydroxylated

A

pro and lys

39
Q

hydroxylated pro forms

A

h bonds between chains

40
Q

hydroxylated lys forms

A

covalent bonds between chains

41
Q

pro and lys residues become hydroxylated reuiqres

A

vitamin C

42
Q

the collagen in tendons are arranged as

A

parallel bundles

43
Q

the collagen in skin are arranged in

A

sheets of fibrils lyaered at many angles

44
Q

the collagen in cartilage has

A

no distinct arrangement

45
Q

cornea collagen is

A

planar sheats stacked corssways to minimize light scatter

46
Q

_________is the overall 3d structure of the folded peptide

A

tertiary structure

47
Q

globular proteins fold during and following synthesis along the same principles as

A

micell formation

48
Q

what are some forces that can stabilize structures of globular proteins

A

electrostatic attractions
hydrogen bonds
hydrophobic interactions
disulfide bonds

49
Q

________assist in protein folding by slowing it down to prevent inapprorpiate interactions

A

molecular chaperones

50
Q

_____________are protein conformational diseases caused by misfolded proteins

A

prion diseases

51
Q

what protein structure is messed up in prion diseases

A

tertiary structure

52
Q

_____________are domains that are physically independent regions within the overall tertiary structure of a large complex protein

A

structural domains

53
Q

polymorphisms, protein families isoforms, and developmental variation are all examples of

A

variations in primary structure

54
Q

_____________ are variations in primary structure of 2 or more alleles may be silent some have a profound effect

A

polymorphisms

55
Q

_________-are proteins with simila but NOT identical structure and function that have evolved from the same ancestral protein; sequences very similar

A

protein families

56
Q

examples of protein families

A

hemoglobin chains, myoglobin serine proteases

57
Q

_____________perform essentially the same function and are highly homologus and evolved from the same ancestral gene possess different amino acid sequences and physico-chemical properties

A

protein isoforms

58
Q

___________are different isoforms that are expressed during different stages of development

A

developmental variation

59
Q

__________are highly similar sequences that evolved from the same ancestor

A

homologs

60
Q

____________are from different species but orignated from same gene in ca common ancestor and normally retain same function

A

orthologs

61
Q

example of orthologs

A

human bovine and procine insulin

62
Q

___________from same species, originated from common ancestral gene, have different functions ( myogloin and different hemoglobin chains)

A

paralogs

63
Q

fetal hb have what structure

A

alpha 2 gamma 2

64
Q

adult hb have what structure

A

alpha 2 beta 2 or alpha 2 delta 2

65
Q

gower I

A

zeta 2 epsiolon 2

66
Q

gower II

A

alpha 2 epsiolon 2

67
Q

protalnd I

A

zeta 2 gamma 2

68
Q

________is the aggregation of an interaction between subunits in a multimeric protein

A

quatenary structure

69
Q

human hemoglobin differences are examples of

A

paralogs

70
Q

does myoglobin have a higher or lower affinity for oxygen

A

myoglobin

71
Q

in the absence of oxygen hemoglobin is predominantly in the

A

T state

72
Q

when oxygen binds all four subunits change to the ________ state

A

R state

73
Q

binding of myoglobin is

A

noncooperative so graph is hyperbolic

74
Q

at a lower pH Hb has a

A

less affinity for the oxygen

75
Q

fetal red blood cells have

A

higher affinity for oxygen than maternal RBC’s

76
Q

2,3 BPG and carbon dioxide both

A

decrease hb affinity for oxygen

77
Q

when proteins denature the structures is lost but

A

primary structure remains in intact

Biochemistry Fall MS1 (12 decks)

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