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CC1 Lab > Amino Acids & Protein > Flashcards

Amino Acids & Protein Flashcards

1
Q

are the building blocks of proteins

A

amino acids

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2
Q

amino acids have __ a code in your amino group, it also has ___ group

A

N terminal, carboxyl group

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3
Q

differs in every amino acids, determines the chemical behavior of that particular amino acid

A

side chain

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4
Q

10 essential amino acids

A

arginine
histidine
isoleucine
leucine
lysine
methionine
phenylalanine
threonine
typhthopan
valine

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5
Q

amino acids with positively charged side chain

A

arginine, histidine, lysine

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6
Q

amino acids with negatively charged side chain

A

aspartic acid, glutamic acid

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7
Q

amino acids with uncharged side chains

A

serine, threonine, asparagine, glutamine

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8
Q

special cases amino acids

A

cysteine, selenocysteine, glycine, proline

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9
Q

amino acid with hydrophobic side chains

A

alanine
isoleucine
leucine
methionine
phenylalanine
tryptophan
tyrosine
valine

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10
Q

protein forming from amino acids starts with

A

a cell

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11
Q

the nucleus contains the ___, it is then split into ___ pairs of chromosome

A

genome, 23 pairs of

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12
Q

each chromosome contains a long strand of __, they are tightly packed around histones

A

DNA

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13
Q

within the DNA are sections called ___ they contain instructions for making proteins

A

genes

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14
Q

when the genes are switched on, an enzyme called ____ attaches to the gene

A

RNA polymerase

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15
Q

RNA polymerase attaches to the gene, it moves along the DNA making a strand of RNA out of 3 bases in the nucleus, the code then determines the order in which the bases are added to the mRNA.

A

transcription

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16
Q

before the mRNA can be used as a template for the production of proteins, it needs to be processed. this involves

A

removing and adding sections of RNA

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17
Q

moves out of the nucleus into the cytoplasm

A

messenger RNA

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18
Q

protein factories in the cytoplasm , binds to the mRNA

A

ribosomes

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19
Q

reads the code in the mRNA to produce a chain made up of amino acids

A

ribosome

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20
Q

there are ___ types of amino acids

A

20 types of

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21
Q

carries the amino acids to the ribosome

A

tRNA

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22
Q

mRNA reads ___ bases at a time

A

3 bases

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23
Q

as each triplets are read ___ delivers the corresponding amino acids, which is added to a growing chain of amino acid

A

tRNA

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24
Q

once the last amino acid has been added, the chain folds into a complex 3D shape to form the?

A

protein

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25
Q

amino acids are linked by a ___ thats why proteins are ____

A

peptide bond, polypeptide

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26
Q

polypeptide will fold based on the confirmation depending on the interaction between the

A

amino acid side chain

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27
Q

macromolecules made up of amino acids

A

protein

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28
Q

most of your proteins are synthesized in the

A

liver

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29
Q

immunoglobulins are synthesized in the

A

plasma cells

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30
Q

only contains amino acids and peptide bonds

A

simple proteins

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31
Q

combination of amino acids plus non protein group

A

conjugated proteins

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32
Q

carry lipid (carriers) considered as conjugated because it has amino acid but also contain a non protein

A

lipoprotein

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33
Q

diff shapes of protein

A

fibrous, globular, simple globular

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34
Q

fibrous proteins

A

fibrinogen, streponins, collagen

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35
Q

globular proteins

A

hgb, plasma, proteins, enzymes, peptide hormones

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36
Q

are compact, meaning they have little or no space for water in that molecule

A

simple globular proteins

37
Q

tissue nutrition

A

energy

38
Q

maintenance of water distribution between cells and tissue, interstitial compartments, and the vascular system of the body

A

osmotic force

39
Q

participation as buffers to maintain pH

A

acid base balance

40
Q

metabolic substances

A

transport

41
Q

part of immune defense system

A

antibodies

42
Q

hormones and receptors

A

hormones

43
Q

connective tissue

A

structure

44
Q

catalysts

A

enzymes

45
Q

participation in coagulation of blood

A

hemostasis

46
Q

basis of folding will depend on the side chain of the amino acids which is your

A

R

47
Q

4 structures of protein

A

primary, secondary, tertiary, quarternary structure

48
Q

linear sequence of amino acids, but this structure can already determine the identity of protein, the molecular structure, the binding capacity and recognition ability

A

primary structure

49
Q

a repeating structure. it involves the winding of your polypeptide chain. it can form sheets which are called beta pleated sheets it could also curl which is called an alpha helix

A

secondary structure

50
Q

it can add strength and flexibility to your protein

A

secondary structure

51
Q

there is a 3D configuration, there is a folding pattern of your protein, this is responsible for the many chemical and physical properties of your protein

A

tertiary structure

52
Q

functions of protein

A

energy, osmotic pressure, acid base balance, transport, antibodies, hormones, structure, enzymes, hematosis

53
Q

secondary structure can form sheets which are called

A

beta pleated sheets

54
Q

secondary structure can also curl which is called an

A

alpha helix

55
Q

there are associations of 2 or more polypeptide chains. this forms a functional protein molecule

A

quarternary structure

56
Q

can determine the identity, molecular structure, binding capacity and recognition ability

A

primary structure

57
Q

responsible for the many chemical and physical properties of protein

A

tertiary structure

58
Q

a principal fetal protein which is used to assess maternal serum as screening test for any fetal conditions

A

alpha fetoprotein

59
Q

has the highest concentration of plasma

A

albumin

60
Q

if we test for proteins we test

A

total protein - albumin = globulins

61
Q

indicator of nutrition, binds thyroid hormones and retinol binding protein

A

prealbumin

62
Q

binds bilirubin, steroids, fatty acids, major contributor to oncotic pressure

A

albumin

63
Q

acute phase reactant, protease inhibitor

A

alpha 1 antitrypsin

64
Q

elevated levels of alpha fetoprotein indicates risk for

A

spina bifida

65
Q

acute phase reactant, may be related to immune response

A

alpha 1 acid glycoprotein (orosomucoid)

66
Q

transport lipids (HDL)

A

alpha 1-lipoprotein

67
Q

inhibits serine proteinases

A

alpha 1 antichymotrypsin

68
Q

component of leukocyte antigen (HLA) molecules

A

B2-microglobulin

69
Q

immune responses

A

c1q, c3, c4 complement

70
Q

precursor of fibrin clot

A

fibrinogen

71
Q

acute phase reactant, motivates phagocytosis in inflammatory disease

A

C-reactive protein (CRP)

72
Q

antibodies

A

immunoglobulin G, A, M, E, D

73
Q

antibodies in secretions

A

immunoglobulin A

74
Q

antibodies in early response

A

immunoglobulin M

75
Q

antibodies in reagins and allergy

A

immunoglobulin E

76
Q

transports iron

A

transferrin

77
Q

binds heme

A

hemopexin

78
Q

most common acute phase reactant, oxidase activity, contains copper

A

ceruloplasmin

79
Q

ceruloplasmin is also a marker for

A

wilson’s disease

80
Q

LDL is a?

A

beta globulin

81
Q

rough measure of all the proteins in the plasma

A

total proteins

82
Q

total protein low result

A

hypoproteinemia

83
Q

states that there is a negative nitrogen balance, there is more catabolism breakdown and there is combination or growth than anabolism

A

hypoproteinemia

84
Q

high total protein

A

hyperproteinemia

85
Q

a result of dehydration or excessive production of protein

A

hyperproteinemia

86
Q

clinical adult range of total protein

A

6.5-8.3 g/dL

87
Q

is not a part of routine examination

A

protein examination

88
Q

is a big NO because it may falsely elevate the total protein

A

hemolyzed sample

89
Q

is preferred rather than plasma, because anticoagulant slowly dilutes the proteins in the plasma

A

serum

CC1 Lab (8 decks)

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