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Flashcards in Proteins Deck (80):
1

Set of all the proteins expressed by an individual cell at a particular time

Proteome

2

Except for this amino acid, each amino acid has a carboxyl grp, amino grp and distinct side chain

Proline

3

The structure of the _______ dictates the function of amino acid

R group

4

Hydrogen bonds are through attachment to these elements

Sulfur
Nitrogen
Oxygen

5

What type of amino acids forms hydrogen bonds?

Polar uncharged

6

What type of amino acids forms ionic interactions?

Charged amino acids

7

What type of amino acids forms hydrophobic interactions?

Non-Polar

8

Charged amino acids

HAGAL

Histidine
Aspartate
Glutamate
Arginine
Lysine

9

Polar uncharged amino acids

Serine, threonine, tyrosine
Cysteine
Asparagine, Glutamine

10

Amino acid with smallest side chain

Glycine

11

Amino acid used in the 1st step of heme synthesis

Glycine

12

Carrier of ammonia and carbons of pyrivate from skeletal muscle to liver

Alanine

13

Branched chain amino acids

Valine
Leucine
Isoleucine

14

Branched chain amino acids are Metabolites that accumulate in what disease

Maple syrup urine disease

15

Precursor of tyrosine

Phenylalanine

16

Accumulates in phenylketonuria

Phenylalanine

17

Largest side chain amino acid

Tryptophan

18

Amino acid with double ring

Tryptophan

19

Tryptophan derivatives

Trip Mo Siya Noh

Melatonin
Serotonin
Niacin

20

Precursor of homocysteine

Methionine

21

Not an amino acid but an imino acid

Proline

22

Tyrosine derivatives

Pare True Love Does Not Exist To Melanie

Phenylalanine
Tyrosine
L- dopa
Dopamine
Norepi
Epinephrine
Thyroxine
Melanin

23

Amino acid involved in ammonia formation

Glutamine

24

Amino acid that participates in the biosynthesis of coenzyme A

Cysteine

25

Cystine contains a lot of

Keratin

26

Precursor of GABA and glutathione

Glutamate

27

Precursor of histamine

Used in diagnosis of folic acid deficiency

Histidine

28

Precursor of crea, urea and NO

Arginine

29

21st amino acid

Selenocysteine

30

All amino acids are chiral except for

Glycine

31

Amino acid that bears no charge at its isoelectric pH

Zwitterion

32

Amino acid that is considered nutritionally semi essential

Arginine

33

Arginine can be synthesized in what pathway

Urea cycle

34

Essential amino acids

PVT TIM HALL always Argues never Tyres
Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Histidine
Arginine
Leucine
Lysine

35

This protein structure is determined by a protein's amino acid sequence

Primary structure

36

Partial double bonds that are generally in the trans configuration

Peptide bonds

37

Process of identifying the specific amino acid at each position in the peptide chain

Sequencing

38

First protein to be sequenced

Insulin

39

Folding of short continuous segments of polypeptides into geometrically ordered units

Secondary structure

40

Most common secondary structure

Spiral with polypeptide backbone core

Alpha helix

41

Amino acid residues that form a zigzag or pleated pattern

Beta sheet

42

Supersecondary structures produced by packing side chains from adjacent secondary elements

Motifs

43

Also called 3D shape of a protein

Tertiary structure

44

Fundamental functional and 3D structural units of polypeptide

Domains

45

Specialized group of proteins required for proper folding and prevent aggregation

Chaperones

46

Results in unfolding and disorganization of the protein's secondary and tertiary structure

Denaturation

47

Most common and important degenerative disease of the brain

Amyloid plaque
Neurofibrillary tangles

Alzheimers

48

This lipoprotein is implicated in the conformational transformation of beta amyloid

Apo E

49

Heme protein present in heart and skeletal muscle

Myoglobin

50

O2 dissociation curve of hemoglobin and myoglobin

Hemoglobin- sigmoidal
Myoglobin- hyperbolic

51

Factors that cause the hemoglobin dissociation curve to shift to the right

CABET
Increased
CO2
Acidity
2,3 BPG
Exercise (O2 demand)
Temperature

52

The release of oxygen from hemoglobin is enhanced when the pH is lowered or when in the presence of increased pCO2

Bohr effect

53

Describes when less O2 is bound, the affinity of hemoglobin to CO2 increases

Haldane effect

54

Hemoglobin A is seen when the baby is this age

8 months old

55

Site of hemoglobin in sequence

Yolk sac
Liver
Marrow

56

Form of hemoglobin bound to carbon monoxide in place of oxygen

Carboxyhemoglobin

57

Hemoglobin that has increased affinity for cyanide

Methemoglobin

58

Also called chocolate cyanosis

Methemoglobinemia

59

Treatment for cyanide poisoning

Methylene blue

60

Mutation in hereditary spherocytosis

Ankyrin
Spectrin

61

Sickle cell disease is from a point mutation in genes

The amino acids interchanged are

Valine and glutamate

62

Hemoglobin C disease happens when these are interchanged

Lysine and glutamate

63

Which chromosome is affected in alpha thalassemia?

Chr 16

64

Which chromosome is affected in beta thalassemia?

Chr 11

65

Most abundant protein in the body

Collagen

66

Most common type of collagen

Type 1

67

Type of collagen in bone and tendon

Type 1

68

Type 2 collagen is found in

Cartilage

69

Type of collagen found in reticulin:
Skin, blood vessels, uterus

Type 3

70

Type 4 collagen is found in the

Basement membrane

71

Inherited disorder of collagen characterized by hyperextensibility of skin, increased joint mobility

Ehlers Danlos

72

Most common type of Ehlers Danlos

Hypermobility type

73

Most serious type of Ehlers Danlos

Vascular type

74

Ehlers Danlos has a defect in what type of collagen?

Type 3 - most common
Type 1
Type 5

75

Defect in type 1 collagen
Brittle bone disease
Autosomal dominant

Osteogenesis imperfecta

76

Genetic disorder where there is a defect in type 4 collagen

Alport syndrome

77

Main presenting sign of Alport
Syndrome

Hematuria

78

Copper deficiency resulting to kinky hair and growth retardation

Menkes disease

79

Autosomal dominant
Mutation in fibrillin gene

Marfan

80

Emphysema may be due to this deficiency

Alpha 1 anti trypsin