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BIOCHEM > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

polymers unbranched chains of amino acids present

A

Protein

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2
Q

% of protein in cell’s mass
% of nitrogen content

A

15%
15.4%

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3
Q

composition of protein

A

carbon, hydrogen, nitrogen, oxygen & sulfur

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4
Q

None of standard amino acids are chiral : T/F

A

True

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5
Q

has 20 alpha amcid; found in proteins

A

Standard amino acid

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6
Q

nonpolar amino acids are:

A

hydrophobic & found in interior of protein

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7
Q

polar amino acids are:

A

hydrophilic

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8
Q

3 polar amino acids

A

neutral
acidic
basic

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9
Q

has carboxyl group part of side chains ; 2 amcid

A

acidic

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10
Q

has 1 amino group part of side chain ; 3 amcid

A

basic

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11
Q

has 6 amino acids

A

neutral

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12
Q

3 letter naming amcid

A

Nomenclature

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13
Q

1 letter nomenclature

A

computing amcid sequence

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14
Q

Chirality of amcid

A

4 diff groups attach to alpha carbon atom except glycine (r group is hydrogen)

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15
Q

amino acids in nature/proteins are:

A

L-isomers

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16
Q

give up protons ; - charged species

A

Carboxyl groups

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17
Q

accept protons ; + changed species

A

Amino groups

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18
Q

ph where amcid exist in zwitter form

A

Isoelectric point

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19
Q

3 types of peptide

A

Dipeptide
Oligopeptide
Polypeptide

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20
Q

covalent bonds between amcids

A

Peptide bonds

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21
Q

peptide w same amcid but present in diff order

A

Isometric peptide

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22
Q

small peptide hormones

A

Oxytocin & vasopressin

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23
Q

Regulate uterin contractions

A

Oxytocin

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24
Q

regulate secretion of water

A

Vasopressin

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25
Q

pentapeptide neurotransmitters by the brain ; bind receptor sites

A

Enkephalins

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26
Q

tripeptide in high levels in most cells

A

Glutathione

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27
Q

has unusual structure feature; regulates oxidation; protects cellular contents from agents

A

Glutathione

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28
Q

Structure of gluta

A

Glu bonded to cys through side chain carboxyl group

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29
Q

protein classification:

A

Simple & conjugated protein

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30
Q

1/more amcid & POLY CHAIN (prostetic groups present) (PROTEIN)

A

Conjugated

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31
Q

protein w carbohydrate group

A

glycoprotein

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32
Q

structures of protein:

A

Primary, secondary, tertiary & quarternary

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33
Q

order where amcid are linked together in protein

A

Primary structure

34
Q

he sequenced primary structure of first protein (insulin)

A

Frederick Sanger

35
Q

planar, has rigidity

A

Peptide linkages

36
Q

arrangement adopted by backbone portion of a protein

A

Secondary protein structure

37
Q

structure (coiled spring)
maintained by hydrogen bonds ; right handed

A

Alpha helix structure

38
Q

2 fully extended protein segments in mol ; arizes from zigzag pattern

A

Beta pleated sheets

39
Q

3 dimentional shape of protein l widely separated

A

Tertiary structure

40
Q

occur between acids w polar r groups

A

Hydrogen bond

41
Q

2 nonpolar chains close to each other

A

Hydrophobic attractions

42
Q

organization of peptide units in multimeric protein

A

Quarternary structure

43
Q

results in regeneration of amino & carboxyl

A

Protein hydrolysis

44
Q

absorbed in blood stream to new proteins

A

free amino acid

45
Q

disorganizations of proteins 3d shape

A

Protein denaturation

46
Q

Precipitation of denaturated protein

A

Coagulation

47
Q

protein mol w peptide chain into spherical shape ; water soluble

A

Globular proteins

47
Q

proteins w elongated shapes

A

fibrous proteins

48
Q

most abundant protein in humans (30%)

A

Collagen

49
Q

structure of collagen

A

triple helix (maintained by glycine & proline)

50
Q

oxygen carrier mol in blood ; tetramer

A

Hemoglobins

51
Q

oxygen storage molecule in muscles ; higher affinity than hemo

A

Myoglobins

51
Q

CLASSIFICATION FUNCTIONOF PROTEINS

A

Catalyst
Defense
Transport
Messenger
Contractile
Structural
Transmembrane
Nutrient
Buffer
Fluid balance
Storage
Regulatory

51
Q

Defense Function ex:

A

immunoglobulins/antibodies

52
Q

Messenger function ex

A

insulin, glucagon

53
Q

(function) Form of movement

A

Contractile

54
Q

ex of Contractile

A

actin, myosin; human repro

55
Q

Structural ex

A

Collagen, cartilage, keratin

56
Q

transmembrane (function)

A

control movement of small mol & ions

57
Q

Storage exampls

A

Feritin & Myoglobin

58
Q

(function) exterior surface of cell membranes ; enzymes

A

Regulatory

59
Q

(function) important from embryo to infant

A

Nutrient

60
Q

Nutrient examples (function)

A

Casein ; Ovalbumin (eggwhite)

61
Q

maintains acid balance (function)

A

Buffer

62
Q

has carbohy derivatives addition to amcid

A

Glycoproteins

63
Q

Structual feature of Collagen

A

4 hydroxyproline & 5 hydroxylsine

64
Q

protective response to invasion of microorganism

A

Immunoglobulins

65
Q

foreign substance ; bacteria/virus

A

Antigen

66
Q

biochem mol counteracts w antigen

A

Antibody

67
Q

suspends lipid & transports them through blood stream

A

Lipoproteins

68
Q

transport system ; spherical feature ; central core of lipid material

A

Plasma lipoproteins

69
Q

Classes of Plasm Lipoproteins

A

Chylomicrons
Very low density Lipoproteins
Low density lipoproteins
High denisty lipoproteins

69
Q

transport dietary glycerols

A

Chylomicrons

70
Q

Transport triacyl synthesized

A

Very low density lipoproteins

71
Q

Transport cholesterol synthesized

A

Low density lipoproteins

72
Q

collect excess cholesterol from body tissues

A

High density Lipoprotein

73
Q

amcid producing disulfied bonds

A

cysteine-cysteine

74
Q

polypeptide chains in beta pleated sheet conformation are held by

A

hydrogen bonding

75
Q

some simple proteins are conjulated proteins: T/F

A

TRUE

76
Q

standard amino acid with out alpha carbon

A

glycine

BIOCHEM (8 decks)

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