Proteins

115 flashcardsby Ash
Study these flashcardsFree · spaced repetition · iPhone, Android, Mac & web

All cards

1
Enzymes are biologically active
  • DNA molecules
  • proteins
  • carbohydrates
  • nucleic acids
2
There are non amino group in proteins, what are they called?
Prosthetic group
3
What color is the hemoglobin when the heme/haem groups are combined with oxygen?
Red
4
What color is the hemoglobin when the heme/haem groups do not have oxygen?
blue or close to purple
5
Fibrous proteins are soluble in water
  • False
  • True
6
A peptide bond is
  • rigid with partial doble bond character
  • planar, covalent
  • all of the above
7
Why is glycine very common in collagen?
  • because it is a simple amino acid
  • because it is large
  • because it's small
8
When the temperature and altitude is low where is the oxygen molecule located? (Bohr's effect)
  • tissues
  • blood
9
When the temperature and altitude is high where is the oxygen molecule located? (Bohr's effect)
  • blood
  • tissue
10
When the pH is low where is the oxygen molecule located
  • blood
  • tissue
11
When the pH is high where is the oxygen molecule located
  • tissue
  • blood
12
Total number of amino acids involved in the protein synthesis of plants
20
13
The 3D structure of protein can be determined by
  • x-ray chrystallography
  • spectroscopy
  • nuclear magnetic resonance
14
Disulfide bonds can be determined by
  • proline residues that are close together
  • histidine residues that are close together
  • cysteine residues that are close together
15
hemoglobin has which structure
  • primary
  • tertiary
  • secondary
  • quaternary
16
Tertiary structure is mainatined by
  • disulphide bond
  • peptide bond
  • all of the above
  • hydrogen bond
17
alpha helix structure has how much amino acid residues/turn?
  • 3.6
  • 3.4
  • 3.8
18
Fibrous proteins such as silk fibroin consists of polypeptide chains arranged in
  • beta pleated sheets
  • alpha helix
19
Myoglobin is a protein with
  • tertiary structure
  • secondary structure
  • quaternary structure
  • primary structure
20
What is the most common secondary structure
alpha-helix
21
What are the two classification of proteins
globular and fibrous
22
the classification of proteins depends on
  • none of the above
  • type of amino acid
  • structure and function
  • numbers of amino acid
23
How many amino acids does insulin contain?
51
24
The first protein sequnced by Frederick Sanger
  • myoglobin
  • myosin
  • hemoglobin
  • insulin
25
The structure of protein can be destroyed by which rays?
  • infrared rays
  • radio waves
  • ultraviolet rays
  • micro waves
26
Which protein is most abundant in the animal world
  • hemoglobin
  • keratin
  • RUBISCO
  • collagen
27
What are the most diverse molecules in the cell
  • proteins
  • lipids
  • mineral salts
  • carbohydrates
28
Amino acids are joined by
  • glycosidic bond
  • ionid bond
  • peptide bond
  • hydrogen bond
29
The repeating units of proteins are
  • glucose units
  • amino acids
  • peptides
  • fatty acids
30
The oxygen in the carboxylic group of an alpha helix structure bonds to where so that the helix structure form?
to the hydrogen of the amine group 4 places ahead of it
31
What bonds compose the 2 secondary structures?
Hydrogen bonds
32
What are the 2 shapes of secondary structure
alpha helix and beta pleated sheets
33
What reaction happens whe you join amino acids together?
Condensation reaction
34
All proteins are enzymes and all enzymes are proteins
  • true
  • false
35
Proteins responsible for muscle contractions
Actin and myosin
36
Protein found in nails, hair, and surface of the skin
Keratin
37
Protein that strengthens skin
collagen
38
Proteins found in blood
Hemoglobin and myoglobin
39
What is the nature of peptide bond
  • Covalent
  • hydrogen
  • metallic
  • Ionic
40
Which of the following is a 39-residue hormone of the anterior pituitary gland?
  • Glucagon
  • Bradykinin
  • Insulin
  • Corticotropin
41
The average molecular weight of an amino acid residue in a protein is about
  • 128
  • 120
  • 110
  • 118
42
Which part of amino acid gives its uniquness?
  • carboxyl group
  • side chain
  • amino group
43
Which of the followin is not the classified form of conjugated proteins
  • complete proteins
  • glycoproteins
  • lipoproteins
  • metalloproteins
44
Unfolding of a protein can be termed as
  • reduction
  • renaturation
  • oxidation
  • denaturation
45
Which of the following is not a factor responsible for the denaturation of proteins
  • heat
  • charge
  • pH change
  • organic solvents
46
Two chains of amino acids in an insulin molecule are held together by
  • covalent linkage
  • sulfide bridges
  • peptide bonds
  • disulfide bridges
47
tertiary conformation of proteins is maintained by 3 types of bonds namely ionic, hydrogen and...?
  • sulfide
  • covalent
  • disulfide
  • peptide
48
Identify the wrong statement
  • hemoglobin is a fibrous protein
  • hemoglobin is a globular protein
  • collagen is a fibrous protein
  • fibrous proteins are insoluble in water
49
The 3D structure of proteins, folding and shaping is done by
  • polar interactions
  • hydrophobic interactions
  • none of these
  • hydrogen bonding
50
Claeaving of peptide chain is done by
  • arginine
  • tyrosine
  • tryptophan
  • trypsin
51
Which of the following is the correct order of sequencing
  • sequencing, orderig, cleaving
  • ordering, cleaving, sequencing
  • Cleaving, sequencing, ordering
  • ordering, sequencing, and cleaving
52
Edman degradation is used for
  • Identifying C-terminal amino acids
  • identifying N-terminal amino acids
  • Identifying amino acid
  • identiying carbohydrates
53
a coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is
  • tertiary structure
  • B-pleated sheets
  • primary structure
  • a-helix
54
A structure that has hydrogen bonds between polypeptide chains arranged side by side is
  • tertiary stucture
  • primary structure
  • B-pleated sheets
  • a-helix
55
Which of the following is known as helix breakers
  • proline and glycine
  • isoleucine and leucine
  • valine
  • threonine
56
Secondary structure is defined by
  • vander waals forces
  • hydrogen bonding
  • ionic bonding
  • covalent bonding
57
Which of the following is a false statement
  • collagen is helical
  • a-keratin is alpha helical
  • a-keratin is a B-pleated structure
  • hemoglobin has a quaternary structure
58
Fibroin is rich in
  • alanine and glycine
  • proline
  • glycine
  • alanine
59
which of the following bonds are not involved in tertiary type of protein structure
  • hydrogeen bonding
  • salt bridges
  • disulfide bond
  • hydrophilic interactions
60
Which of the following does not posses a quaternary structure
  • creatine phospho kinase
  • myoglobin
  • lactate dehydrogenase
  • immunoglobin M
61
Which of the following is abundantly found in collagen
  • glycine
  • tryptophan
  • serine
  • alanine
62
Which of the following is first determined as oligomer
  • keratin
  • collagen
  • myoglobin
  • hemoglobin
63
Which of the following enzyme is secreted by the pancreas
  • ribonuclease
  • myoglobin
  • lyzozyme
  • cytochrome c
64
Which of the following is false
  • ribonuclease has SH-SH linkage
  • heme group in the cytochrone c is covalently linkes to the protein on two sides
  • ribonuclease has S-S linkage
  • lyzozyme has S-S linkage
65
Which of the followin forces is favorable for protein folding?
  • hydrogen bonding
  • hydrophobic interactions
  • vander waals forces
  • ionic bonding
66
A process by which a protein structure assumes its functional shape or conformation is?
  • folding
  • hydrolysis
  • synthesis
  • denaturing
67
Process of protein folding does not depend on
  • pH
  • solute
  • concentration of salts
  • solvent
68
Whhich of the following cannot denature a protein
  • SDS detergent
  • iodoacetic acid
  • Urea
  • HEating to 90 degrees
  • all can denature proteins
69
Protein which play important roe in folding of proteins int 3D structure
  • transposons
  • folding proteins
  • chaperons
  • satellite proteins
70
contractile protein of a muscle is
  • Myosin
  • Troponin
  • Tropomyosin
  • Tubulin
71
which of the following contractile protein of skeletal muscle involve in ATPase activity?
  • Troponin
  • tropomyosin
  • myosin
  • tubulin
72
the cross bridges involved in muscle contraction are located on the
  • myosin myofilaments
  • actin myofilaments
  • dystrophin
  • tropomyosin
73
Which of the following is false
  • functional unit of muscle is sacromere
  • the band in a myofibril is an area of thin filament
  • actin is a thin filament
  • myosin is a thick filament
74
The connective tissue that surrounds individual fibers is
  • fascia
  • perimysium
  • endomysium
  • epimysium
75
Which of the following is an invagination of the muscle cell's sacrolemma
  • cisternae
  • microtubules
  • T-tubules
  • sacroplasmic reticula
76
What configuration does L-amino acid have?
S-configuration
77
Isoleucine and threonine contain a third stereocenter. True of false?
False
78
Which amino acid has a secondary structure for its alpha amino group?
Proline
79
What type of amino acids do the 20 amino acids have
  • beta amino acids
  • alpha amino acids
80
the alpha carbon of each amino acid is a sterocenter except for
Glycine
81
Protein used as an artificial sweetener that is 200 times sweeter than sugar
aspartame
82
what is the IUPAC name of aspartame
L-aspartyl-L-phenylalanine methyl ester
83
What protein is used to induce labor in pregnant women?
Oxytocin
84
Protein that controls blood pressure by regulating contraction of smooth muscle
Vasopressin
85
Proteins are polymorphic in how much percentage?
  • 10-15%
  • 15-30%
  • 20-30%
86
The linear sequence of amino acids joined together by peptide bonds is termed the secondary structure of the protein.
  • False
  • True
87
Molecules are bound to the column via specific interactions for a bound ligand. Once nonbinding proteins are removed, the protein of interest can be eluted.
  • affinity chromatography
  • gel filtration chromatography
  • ion exchange chromatography
  • dialysis
  • electrophoresis
88
Which of the following techniques is used to separate proteins based upon differences in their mass?
  • Western blotting
  • dialysis
  • Isoelectric focusing
  • SDS-gel electrophoresis
  • Ion-exchange chromatography
89
Hemoglobin and myoglobin are the two oxygen-binding proteins present in large multicellular organisms. Hemoglobin transports oxygen in the blood and is located in the leukocytes; myoglobin stores the oxygen in the muscles.
  • False
  • True
90
Collagen is the name given to a family of structurally related proteins that form strong insoluble fibers.
  • True
  • False
91
The heme prosthetic group consists of a protoporphyrin IX ring and a central Fe3+ atom which forms four bonds with the porphyrin ring.
  • False
  • True
92
All of the following statements describe characteristics of the peptide bond EXCEPT
  • it demonstrates no rotation around the bond
  • it is planar
  • it is polar but uncharged
  • it has a trans configuration
  • it forms a single bond directly linking the α-carbons of adjacent amino acids
93
All of the following statements about hydrogen bonds are true, except
  • It is a type of non-covalent bond.
  • The acceptor must contain a non-bonded pair of electrons.
  • The donor is a hydrogen atom bonded to a less electronegative atom than hydrogen.
  • The more linear the bond, the stronger the attraction.
  • All of these statements describe hydrogen bonds.
94
When proteins denatured in sodium dodecyl sulfate (SDS) and mercaptoethanol are separated by electrophoresis,
  • the direction of electrophoretic movement is positive to negative
  • disulfide bridges are maintained
  • cations of SDS bind to the protein
  • the denatured proteins have a large net negative charge
  • the native protein charge is significant
95
A bond that contributes to forming the secondary structure of proteins but not the primary structure
  • hydrogen
  • peptide
  • ionic
  • hydrophobic
  • disulfide
96
Molecules with a specific charge are selectively bound to a column, separated from proteins that don’t bind, and then eluted.
  • gel filtration chromatography
  • electrophoresis
  • dialysis
  • ion exchange chromatography
  • affinity chromatography
97
The substitution of valine for glutamate at position 6 on the two β-chains in sickle cell hemoglobin causes all the following EXCEPT
  • decreased solubility of deoxyhemoglobin
  • brittle red blood cells
  • decreased electrophoretic mobility at pH 7.0
  • polymerization of deoxyhemoglobin
  • altered primary structure
98
A covalent bond that can be involved in forming the tertiary structure of proteins once they are synthesized
  • disulfide
  • ionic
  • hydrogen
  • hydrophobic
  • peptide
99
Hemoglobin has quaternary structure as it is made up of four polypeptide chains; two α-chains and two β-chains (α2β2), each with a heme prosthetic group.
  • True
  • False
100
Quaternary structure refers to the spatial arrangement of the polypeptide subunits and the nature of the interactions between them.
  • False
  • True
101
A decreased affinity of hemoglobin for oxygen may result from all the following except
  • initial binding of oxygen to one of the four sites available in each deoxyhemoglobin molecule
  • high carbon dioxide levels
  • a. high pH
  • high 2,3-diphosphoglycerate levels within erythrocytes
  • acidosis
102
Denaturation is brought about by ALL of the following EXCEPT:
  • extremes of pH
  • SDS
  • heat
  • none of these
  • mercaptoethanol
103
Cyanogen bromide (CNBr) cleaves proteins
  • after positively charged residues, such as K and R
  • after aromatic residues, such as Y and W
  • after negatively charged residues, such as D and E
  • after valine residues
  • after methionine residues
104
In comparing the secondary structure of proteins, it can be seen that all the following descriptions apply only to a β-sheet and not to an α-helix except
  • it is composed of two or more segments of polypeptide chain
  • N terminals of chains are together and parallel
  • chains are almost fully extended
  • N-terminal and C-terminal ends of chains alternate in an antiparallel manner
  • all peptide bond components participate in hydrogen bonding
105
All the following statements describing protein structure are true except
  • intrachain disulfide bonds are usually extremely important in determining the folding of a newly synthesized protein
  • charged amino acid side chains tend to be on the outside of folded proteins
  • primary structure is one of the most important factors determining the higher order structure of proteins
  • hydrophobic amino acid side chains are usually found within the center of protein molecules
  • many proteins have no quaternary structure
106
A protein is a linear sequence of amino acids linked together by glycosidic bonds.
  • True
  • False
107
Which of the following states of hemoglobin (Hb) binds oxygen with the greatest affinity?
  • Hb(O2)2
  • Hb(O2)
  • Hb(O2)3
  • Hb(O2)4
  • Hb
108
Which of the designations below best describes the relationship of subunits in the quaternary structure of adult hemoglobin?
  • (α1 – α2) (β1 – β2)
  • α1 – α21 – α2 – α3 – α4
  • (β1 – β2 – β3 – α1)
  • (α1 – β1) - (α2 – β2)
  • α – β – β – α
109
Which one of the following statements correctly descries transport of oxygen by hemoglobin?
  • The plot of percentage of oxygen bound versus oxygen pressure is sigmoidal in shape.
  • Each of the four heme moieties binds oxygen independently.
  • Increased carbon dioxide concentrations increase oxygen affinity.
  • The binding of oxygen to hemoglobin causes a valence change in the iron of the heme moiety.
  • Oxygen binds to hemoglobin more avidly than does CO.
110
All the following are important in determination of the primary structure of a protein except
  • determination of the number of polypeptide chains
  • determination of the amino acids sequence in peptide fragments
  • cleavage of pure polypeptide chains to smaller chains
  • separation of different polypeptide chains
  • determination of the extent of α-helix formation
111
Which of the following techniques for purification of proteins can separate proteins by size?
  • gel filtration chromatography
  • ion exchange chromatography
  • affinity chromatography
  • dialysis
  • isoelectric focusing
112
Salting out with ammonium sulfate is based upon proteins interacting with other proteins via
  • hydrogen bonds
  • ionic bonds
  • hydrophobic interactions
  • hydrophilic interactions
  • disulfide bonds
113
Primary structure in a protein refers to the three-dimensional arrangement of all the amino acids in the polypeptide chain.
  • False
  • True
114
Molecules are separated based on its isoelectric points.
  • cation exchange chromatography
  • electrophoresis
  • isoelectric focusing
  • gel filtration chromatography
  • affinity chromatography
115
Which of the following techniques for purification of proteins can be made specific for a given protein?
  • dialysis
  • affinity chromatography
  • gel filtration chromatography
  • electrophoresis
  • ion exchange chromatography
Study all 115 cards for free