問題一覧
1
describes the role of disulfide bonds in protein structure
contribute to the tertiary structure of proteins
2
NOT a common mechanism employed by chaperones
directly catalyzing the formation of peptide bonds
3
forces primarily drives protein folding
hydrophobic interactions
4
Mutation that disrupts disulfide bond that lead to loss of function
loss of tertiay structure stability
5
Single amino acid substitution in hemoglobin can cause sickle cell anemia due to
change in tertiart structure of hemoglobin
6
Which of the ff statements about PROTEIN DOMAINS is FALSE
always encoded by single exon
7
Hydrogen bonding pattern in an alpha helix
four residues away
8
Proline residues often disrupts alpha helix because
lack of hydrogen atom on the alpha amino group
9
NOT a common type of interaction in protein binding
covalent bond
10
NOT affect the BINDING AFFINITY
genetic code
11
Common protein motif in DNA binding
all of the above
12
NOT a common mechanism by which enzymes lower activation energy?
increased substrate conc.
13
Which of the following statement is correct about PHENYLALANINE
remains essential amino acid
14
A mutations that alters single amino acid can impact its function. This is primarily due to changes in
tertiary struct.
15
NOT a common post transitional modification that can affect protein function
replication
16
NOT a common mechanism employed by Chaperone
directly catalyzing peptide bonds
17
NOT typically lead to protein denaturation
high substrate conc.
18
Accurately describes the relationship between protein sequence and function
the amino acid sequence determines its 3D structure, which in turn determines its function
19
Missense mutation in a gene encoding a protein can lead to variety of phenotypic edfects.
can alter the protein folding, stability and active site
20
Which of the following statements correctly distinguish between parallel and antiparallel beta sheets
In parallel beta sheets, the adjacent strands run in the same direction, while in antiparallel beta sheets, the adjacent strands run in opposite directions.
21
Factor that can influence the stability of an alpha helix
all of the above
22
A protein domain that specifically recognizes and binds to another protein or molecule is known as
module
23
NOT a common fuction of protein protein interaction
lipid synthesis
24
Which of the following statements about protein domain is FALSE
always encoded by single exon
25
Which of the ff is NOT a common characteristics of competitive inhibation
the inhibitor binds irreversibly to the enzyme
26
Which of the ff is NOT common characteristic of competative inhibation
the inhibitor binds irreversibly to the enzyme
27
Which of the ff essential amino avid plays a crucial role in the synthesis of neurotransmitters like serotonin and melatonin
tryptophan
28
Statements accurately describes a key difference between essential and non essential amino acids
Essential amino acids have a unique side chain structure that cannot be synthesized by human body
29
Which metabolic pathway involves the degradation of amino acid to produce energy or to synthesize glucose
citric acid cycle
30
Deficiency of which essential amino acid can lead to kwashiorkor, severe form of malnutrition characterized by edema, growth retardation and muscle wasting
threonine
31
Which of the ff is not BCAA?
threonine
32
Which tf the ff statement describes the role of peptide bonds protein structure
link amio acid together to form polypeptide chain
33
Peptide bonds directly participate in which of thee ff types of protein protein interactions
covalent bonding
34
Techniques relies on the cleavage of peptide bonds at specific amino acids residue to determine the amino acid sequence
mass spectoscopy
35
Why are peptide bonds highly conserved across different species
essential for the formation of functional proteins and any alteration would disrupts protein structure and function
36
Spectroscopic technique can be used to directly observed the vibrational modes of peptide bonds
IR spectroscopy
37
A singlle amino acid substitution in a protein can impact stability what factor can contribute to this
all of the above
38
Which of the ff types of missense mutations s most likely to have impact in protein funtion
non consevative substitution
39
Which of the ff bioinformatic tools is commonlu used to predict secondary structure of protein
PSIPRED
40
Which of the ff types of immune cells recognize specific amino acid sequence on antigens
t cells
41
Which of the ff amino acid is known to introduce flexibility
glycine
42
Which level of protein structure s primarily determined by hydrogen bonding between the amide and carbonyl
secondary struct
43
Which of the ff essential amino acid has sulfur containing side chaiin
methionine
44
Which amino acid is a precursor for the synthesis of heme
glycine
45
Which of the ff is NOT a potential consequence of long termamino acid defficiency
enhanced cognitive function
46
A defficiency of which essential amino acid can lead to neurological disorder and impaired cognitive function
tryptophan
47
Which of the ff statements about isopeptide bond is correct
ormeed between the side chains of amino acid
48
Which of the ff information can be directly obtained fron xray crytallography data
peptide bond angles and bond length
49
How can the study of conserved peptide motifs help in understandingprotein evolution function
all of the above
50
Which technique can be used to study the kinetic of peptide bondformation
stopped flow spect
51
Which of the ff amino acid substitutions is most likely to have significant impact on protein stability
alanine to proline
52
How cystic fibrosis mutation might affect the structure and function of CFTR protein
all of the above
53
Chou fasman method is a method for predicting protein secondary struct. Which of the ff factor does this method consider
prosperity of amino acid to form alpha and beta
54
Why are ceertain amino acid sequences more immunogenic than others
located in regions of the protein that are exposed to the extracellular environment
55
Howcan amino acid sequence influence the conformational flexibility of a protein
alll of the above
56
A proteins tertiary structure is primarily stabilized by which type of interaction
hydrogen bonds/hydrophobic interactions/ionic bonds
57
Which of the ff informations can be obtained from CD spectroscopy
secondary struct
58
A common experimental technique used to study the folding and insertio of membrane proteins into lipid bilayers
solid state NMR spect
59
Which of the ff statements accurately describes multidomain protein in hierarchcal manner process
each domain folds independently
60
Which of the ff enzymes falls under the category of oxireductases
lactate dehydrogenase
61
Which of the ff enzymes is classified as a hydrolase
amylase
62
Which of the ff enzymes is classified an an isomerase
phosphoglucose isomerase
63
Whichof the ff enzymes exhibits multiclas functionality
alcohhol dehydrogenase
64
Which of the ff enzymes is clinically relevant as a biomarker for liver function and is classified under the oxidoreductase enzyme class
ALT
65
In a lineweaver burk plot,what does y intercept represent
inverse of themaximal velocity (1/Vmax)
66
Which type of enzyme inhibation results in a decrease in Vmax but no chage in Km
competative inhibi
67
Which of the ff best describes role of an allosteric activator in enzyme kinetics
increases substrate binding
68
Which of the ff is an example of covalent modification regulating enzyme activity
phosphorylation
69
Which isoenzyme pair is clinically significant for diagnosing myocardinal infarction
LDH 1 and LDH 5
70
Which of the ff coenzymes is essential in the transfer of one carbon units during metabolic rxn.
NAD+
71
Which of the ff metabolic processes directly utilizes S-adenosylmethionine (SAM) as methyl donor
DNA methylation
72
Which of the ff is a defining characteristic of prosthetic group compared to coenzyme
tightly and permanent
73
Which of the ff is the primary function of het shock protein (HSPs)
preventing protein aggregation
74
Hydrogen-deuterium exchange(HDX) is a technique useed to study protein dynamics aand folding. How HDX work
measures the rate at which hydrogen atoms in a protein exchange withdeuterium atoms
75
Membrane proteins often adopt complex topologies. What is a common mechanism by which these proteins insert into the lipid bilayer
chaperone assisted insertion
76
What is the role of chaperones in folding of multidomain protein
all of the above
77
Whichh of the ff is correct EC(enzyme commission) number classification for oxireductase
EC 1
78
Which rxn is most likely catalyzed by hydrolase
cleavage of a peptide bond
79
Which of the ff best describes the type of rxn catalyzed by isomerase
rearrangement of the molecular structure
80
Which enzyme can exhibit both transferase and hydrolaase activities depending on the substrate or rxn conditions
hexokinase
81
Which enzyme is most commonly used in the industrial production of high fructose corn syrup
isomerases
82
How does a competative inhibitor affect the lineweaver burk plot of an enzyme catalyzed rxn
increases the slope and leaves the y intercept unchanged
83
Which of the ff best describes the effect of an uncompetative inhibator on enzyme kinetics
Km remains unchanged, Vmax decreases
84
How does the sigmoidal curve of an allosterically regulated enzyme differ from the hyperbolic curve of a Michaelis Menten enzyme
represents a cooperative interaction between enzyme subunits
85
How does phosphorylation affect enzyme activity in most regulatory enzyme
can activate or inhibit depending on the enzyme and pathway
86
Which of the ff statements best describe isozymes
enzymes that catalyze the same rxn but differ in their structure and kinetic properties
87
Which of the ff prosthetic groups is tightly bound to the enzyme andis involved in electron transfer
heme
88
Which of the ff compounds is synthesized from S- Adenosylmethionine (SAM) through methylation rxn i the body
acetylcholine
89
Which of the ff is an example of prosthetic group that participate in electron transfer
heme
90
Which of the ff enzymatic rxn involves biotin as prosthetic group
carboxylation of pyruvate to form oxaloacetate
91
Which of the ff best describes the role of FLAVIN ADENINE DINUCLEOTIDE (FAD) and FLAVIN MONONUCLEOTIDE (FMN) in enzymatic rxn
both FAD and FMN act as electron donors in redox rxn
92
Which of the ff is the primay goal of Enzyme Replacement Theraphy (ERT)
replace the deficient or missing enzyme
93
Which of the ff enzymes is most commonly used in the food industry to breakdown starch
amylase
94
A defect in the enzyme 21 hydroxylase leads to an imbalance i which of the ff hormones contributing to congenital adrenal hyperplasia (CAH)
aldoseterone and cortisol
95
Which of the ff statement about biotin as a prosthetic group is correct
covalently bound to the enzyme and assist in the transfer of one- carbon units
96
Which of the ff statements is true regardig Flavin Mononucleotide (FMN) and Flavin Adenine Dinucleotide
both FMN and FAD contains flavin ring structure
97
Which of the ff enzyme is commonly used in Enzyme Replacement Theraphy (ERT) to treat Gauchers disease
imiglucerase
98
In the dairy industry, which enzyme is primarily used to curdle milk and separate curds from whey during cheese production
rennin (chymosin)
99
Which of the ff enzyme defficiencies leads to defect in the synthesis of thyroid hormones, causig a disorder such as congenital hypothyroidism
5- deiodinase