Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

What is the structure of a protein?

A

amino acids joined together by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the 4 types of protein structures?

A

Primary
Secondary
Tertiary
Quaternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

When you consume protein, what needs to be the charge of the amino acid to be absorbed?

A

neutral uncharged AA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Which protein structure has amino acids joined covalently by peptide bonds in a single linear structure?

A

Primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Are hydrogen bonds strong or weak?

A

Strong collectively; individually weak

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Are peptide bonds easy to break

A

Peptide bonds need a combination of a strong acid/base and elevated temperature to break down

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is more stable, cis- or trans- configuration?

A

trans-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why is trans- configuration more stable?

A

Due to steric interference of R-groups in cis- position

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the only charged group on a polypeptide?

A

C- and N-terminals

occasional side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the most common helix?

A

alpha helices

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Why does an alpha helice coil?

A
  • Protected core because orbitals block it

- R Side chains extend outward avoiding steric interference because they are generally large

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Define steric interference

A

stops things from reacting and breaking down the protected core

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What stabilizes a-helices?

A

hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Which 5 amino acids are charged?

A

Glutamate, Asparate, Histadine, Lysine, and arganine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

How does proline disrupt the alpha helix

A

creates kink in chain to create pliability

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is composed of 2 or more peptide chains, segments of polypeptides, or a single polypeptide chain folding back on itself?

A

beta sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are the two types of beta sheet arrangments

A

parallel or anti-parallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Which type of Beta-sheet curl does globular proteins have?

A

Right-handed curl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Which structure do you want to bend? alpha or beta

A

beta bends allowed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What stabilizes beta bends?

A

formation of both ionic and hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Which formation of a beta sheet is most common?

A

anti-parallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is formed by combining secondary structures?

A

supersecondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Why are supersecondary structures helpful?

A

larger molecule means larger characteristics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What structure determines the tertiary structure?

A

primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Which sides of the tertiary structure are hydrophobic and hydrophilic?

A

Hydrophobic interior

Hydrophilic surface

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What is the benefit of tertiary’s surface being hydrophilic?

A

Move through solutions while preventing breakdown.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

All bonds and interactions for proteins are determined by _____________?

A

R side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What causes the folding of tertiary/SS structure

A

R side chains react while also protecting the center and cause internal folding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

How many domains can a protein have?

A

2+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What kind of bond is formed by opposite charges?

A

ionic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

A ________ bond is formed when atoms share valence electrons.

A

covalent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

An _____ bond is formed when one atom accepts or donates one or more of its valence electrons to another atom

A

ionic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What type of bond is formed when atoms don’t share electrons equally?

A

polar covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What type of bond is formed when electrons are shared equally?

A

Nonpolar covalent bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Correctly formed proteins are ____ and have ___ energy states.

A

Stable; low

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Chaperone proteins use what to speed/expand the binding process?

A

Heat

Chaperone proteins=heat shock proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What is the function of chaparones/heat for proteins?

A

Protects proteins as they fold by preventing the exposed regions from being tangled.
aka. catalyst to increase rate of folding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Quaternary structures are held together by _________ interactions

A

noncovalent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

What causes Alzhiemers?

A

1) Basic neurofibular tangles

2) Mutation replicates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Cannibalism causes what disease?

A

prion disease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

What are two types of globular proteins?

A

Myoglobin and Hemoglobin?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What is a complex pf protoporphyrin IX and iron?

A

heme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

Where is the iron located in heme?

A

iron center by 4 nitrogenous bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

What are the 2 additional bonds heme iron can make?

A

1) histadine

2) oxygen or constituents

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Which type of anemia is most common?

A

iron deficiency anemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

What type of structure does myoglobin have?

A

single polypeptide chain of alpha helices

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What can Myoglobin transport?

A

1 molecule of oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Heme group is lined with what charge of amino acids?

A

nonpolar

49
Q

The interior of myoglobin has what bond type of amino acids?

A

Nonpolar/Hydrophobic

50
Q

What bond type of amino acids is located on the surface of myoglobin?

A

Charged

51
Q

What type of globulin protein is found only in RBC?

A

hemeglobin

52
Q

What is the structure of hemeglobin?

A

2alpha + 2beta = 4 polypeptide chains

53
Q

What molecules can hemoglobin transport?

A

O2
CO2
H+

54
Q

What types of bonds stabilizes hemoglobin?

A

hydrophobic, ionic, and hydrogen bonds

55
Q

What types of bonds stabailize myoglobin?

A

hydrogen bonds

56
Q

What is the oxygenation of hemoglobin in the T form?

A

taught = deoxygenated

57
Q

What is the oxygenation of hemoglobin in the R form?

A

relaxed = oxygenated

58
Q

Which globular protein must hit p50 to increase the affinity of binding to oxygen?

A

hemoglobin

59
Q

Which organic phosphate stabilizes hemoglobin and is the most abundant in RBC?

A

2,3-bisphosphoglycerate

60
Q

Explain the 9 step process of oxygenation to and from the lungs

A

1) V pH
2) ^conc CO2
3) mobilize Hemoglobin
4) ^release O2 (return CO2 homeostasis)
- (beta release, alphas hold O2 until T state)
5) ^T form hemoglobin
6) ^CO2 binding off alpha
7) reach p50
8) reach form
9) saturate hemoglobin

61
Q

What is the most abundant organic phosphate in RBCs?

A

2, 3-biphosphoglycerate

62
Q

Which pathway is 2, 3-biphosphoglycerate synthesized in?

A

glycolytic pathway

63
Q

What are the 3 functions of 2, 3-biphosphoglycerate?

A

1) binds hemoglobin and decreases binding affintiy
2) Doesn’t bind oxyhemoglobin
3) Stabilizes taught formation

64
Q

Which formation does the phosphate 2, 3-biphosphoglycerate stabilize?

A

taught

65
Q

Which helice on hemoglobin does 2, 3-biphosphoglycerate bind to?

A

beta-globin chains

66
Q

Which phosphate allows the release of oxygen to the tissues?

A

2, 3-biphosphoglycerate

67
Q

Which minor hemoglobin consists of 2 alpha chains and 2 gama chains?

A

Hb F- Fetal Development

68
Q

What is Hb A1c?

A

Glycosylated hemoglobin

69
Q

Which minor hemoglobin is synthesized in adults at lower concentration than Hb A?

A

Hb A2

70
Q

What is the most common hemoglobin disease?

A

Sickle Cell Disease

71
Q

What is Hb S?

A

sickle cell anemia

72
Q

Who is more common to get sickle cell disease?

A

African Americans

73
Q

What are the symptoms of sickle cell disease?

A

episodes of pain, chronic hemolytic anemia, stroke, splenic and renal dysfunction and increased incidence of infection

74
Q

What causes sickle cell disease?

A

homozoneygous recesive disorder- single nucleotide alteration in beta-globin gene

75
Q

Which disease is Hb C?

A

Hemoglobin C disease

76
Q

Which 2 diseases are caused by structurally abnormal hemoglobin?

A

Sickle Cell Anemia

Hb C disease

77
Q

Which disease is caused by an insufficient synthesis of normal hemoglobin?

A

Thalassemia Syndromes

78
Q

Which disease is a hereditary hemolytic disease?

A

Thalassemia

79
Q

What causes Thalassemia Disease?

A

Imbalance during synthesis of the globin chains

80
Q

Which Thalassemia has a decreased number of a-chains and more b-chains?

A

a-Thalassemia

81
Q

Which Thalassemia has a decreased number of beta-chains and an increased number of alpha chains?

A

b-Thalassemia

82
Q

Which Thalassemia affects the production of functional mRNA?

A

beta-Thalamassia

83
Q

What is the most abundant protein in the body?

A

Collagen

84
Q

What us the form of collagen?

A

3 alpha-chains are wound around one another in a rope like helix

85
Q

What are the 3 types of collagens?

A

1) Fibril-forming collagens
2) Networl-forming collagens
3) Fibril-associated collagens

86
Q

What does Type I Fibril-forming Cartilage form?

A

skin, bone, tendon, blood vessels, corneas

87
Q

What does Type II Fibril-Forming Cartilage form?

A

Cartilage, intervertebral disks, vitreous body

88
Q

What does Type III Fibril-Forming Cartilage form?

A

Blood Vessel, Fetal Skin

89
Q

What is the structure of Type I Fibril-forming Cartilage?

A

High tensile strength, cornea and tendon

90
Q

What is the structure of Type II Fibril-forming Cartilage?

A

Cartilaginous structures

91
Q

What is the structure of Fibril-forming Cartilage is prevalent in more tissues?

A

Type III

92
Q

Which amino acid is located in every 3rd position (most abundant)?

A

glycine

93
Q

Where are the collagen precursor’s formed?

A

fibroblasts

94
Q

Which vitamin works as an activation for collagen formation?

A

Vit C

95
Q

Which mutation leads Ehlers-Danlos Syndrome?

A

Type III mutations or deficiency of collagen processing enzymes

96
Q

What are the results of Ehlers-Danlos syndrome?

A

fragile stretchy skin, loose joints and vascular problems

97
Q

What is another name for brittle bone syndrome?

A

Osteogensis Imperfecta

98
Q

What are the results of osteogensis imperfecta?

A

Bones easily bend , fx, retarded wound healing, twisted spine leading to a humped back

99
Q

Which type of osteogenesis is early onset instantly with fx secondary minor trauma?

A

Type 1

100
Q

Which type of osteogenesis imperfecta is more severe and fatal because of pulmonary hypoplasia in utero?

A

Type 2

101
Q

What rubber like insoluable protein is found in lungs, large arteries and ligaments?

A

elastin

102
Q

Which 2 amino acids is elastin rich in?

A

lysine and proline

103
Q

Which connective tissue disorder causes impaired structural integrity of the skeleton, eye and cardiovascular system?

A

Marfan’s Syndrome

104
Q

Where is a1-Antitrypsin found?

A

contained in the blood and other body fluids

105
Q

Where is a1-Antitrypsin synthesized AND secreted?

A

liver

106
Q

Defective a1-antitrypsin causes what?

A

Emphysema

elasticity destroyed

107
Q

Which protein inhibits: proteolytic enzymes that hydrolize and destroy proteins, trypsin, and neutrophil elastase?

A

a1-Antitrypsin

108
Q

Which diet includes a drastic decrease in carbs that causes a decrease in blood pH (acidic) and causes diuretic effects?

A

Atkins Diet

109
Q

What are 2 diseases caused by protein deficiency?

Which is reversible with an adequate diet?

A

Marasmus and Kwashiorkor

Kwashiorkor

110
Q

Weaning early and going straight to a starchy diet with no protein causes what disease?

A

Kwashiorkor

111
Q

When naming the protein, where is the free amino written?

A

left

112
Q

What is located at the N-terminal in a protein?

A

free amino

113
Q

When naming a protein, where is the free carboxyl written?

A

right

114
Q

What is located at the L-terminal in a protein

A

carboxyl group

115
Q

What unbranched chain is formed from a linkage of many amino acids through peptide bonds?

A

polypeptide

116
Q

What stabilizes alpha helice?

A

hydrogen bonds

117
Q

What is the fundamental functional and 3-dimensional structural unit of polypeptides?
aka. characteristic of a tertiary structure

A

Domain

118
Q

What are the 4 interactions that stabilize tertiary protein structures?

A

1) Disulfied Bomds
2) Hydrophobic interactions
3) Hydrogen Bonds
4) Ionic Interactions

119
Q

Formation of _______ bonds between polar groups on the surface of proteins and the aqueous solvent enhances the solubility of the protein

A

Hydrogen bonds

Biochemistry (11 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions