Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biochem > Proteins > Flashcards

Proteins Flashcards

1
Q

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

A

Proteome

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

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

A

Proline

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

The structure of the _______ dictates the function of amino acid

A

R group

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

Hydrogen bonds are through attachment to these elements

A

Sulfur
Nitrogen
Oxygen

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

What type of amino acids forms hydrogen bonds?

A

Polar uncharged

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

What type of amino acids forms ionic interactions?

A

Charged amino acids

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

What type of amino acids forms hydrophobic interactions?

A

Non-Polar

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

Charged amino acids

HAGAL

A 
Histidine
Aspartate
Glutamate
Arginine
Lysine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Polar uncharged amino acids

A

Serine, threonine, tyrosine
Cysteine
Asparagine, Glutamine

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

Amino acid with smallest side chain

A

Glycine

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

Amino acid used in the 1st step of heme synthesis

A

Glycine

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

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

A

Alanine

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

Branched chain amino acids

A

Valine
Leucine
Isoleucine

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

Branched chain amino acids are Metabolites that accumulate in what disease

A

Maple syrup urine disease

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

Precursor of tyrosine

A

Phenylalanine

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

Accumulates in phenylketonuria

A

Phenylalanine

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

Largest side chain amino acid

A

Tryptophan

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

Amino acid with double ring

A

Tryptophan

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

Tryptophan derivatives

A

Trip Mo Siya Noh

Melatonin
Serotonin
Niacin

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

Precursor of homocysteine

A

Methionine

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

Not an amino acid but an imino acid

A

Proline

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

Tyrosine derivatives

A

Pare True Love Does Not Exist To Melanie

Phenylalanine
Tyrosine
L- dopa
Dopamine
Norepi
Epinephrine 
Thyroxine
Melanin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Amino acid involved in ammonia formation

A

Glutamine

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

Amino acid that participates in the biosynthesis of coenzyme A

A

Cysteine

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

Biochem (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions