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  • 問題数 99 • 12/26/2024

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    問題一覧

  • 1

    Which of the ff amino acid substitutions is most likely to have significant impact on protein stability

    alanine to proline

  • 2

    Howcan amino acid sequence influence the conformational flexibility of a protein

    alll of the above

  • 3

    Which of the following statement is correct about PHENYLALANINE

    remains essential amino acid

  • 4

    Which of the ff is the primary function of het shock protein (HSPs)

    preventing protein aggregation

  • 5

    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

  • 6

    Which of the following statements about protein domain is FALSE

    always encoded by single exon

  • 7

    Mutation that disrupts disulfide bond that lead to loss of function

    loss of tertiay structure stability

  • 8

    NOT affect the BINDING AFFINITY

    genetic code

  • 9

    A common experimental technique used to study the folding and insertio of membrane proteins into lipid bilayers

    solid state NMR spect

  • 10

    How cystic fibrosis mutation might affect the structure and function of CFTR protein

    all of the above

  • 11

    Which of the ff is NOT a potential consequence of long termamino acid defficiency

    enhanced cognitive function

  • 12

    Which of the ff statements accurately describes multidomain protein in hierarchcal manner process

    each domain folds independently

  • 13

    Why are ceertain amino acid sequences more immunogenic than others

    located in regions of the protein that are exposed to the extracellular environment

  • 14

    Which of the ff enzymes is most commonly used in the food industry to breakdown starch

    amylase

  • 15

    Which of the ff statements about PROTEIN DOMAINS is FALSE

    always encoded by single exon

  • 16

    Missense mutation in a gene encoding a protein can lead to variety of phenotypic edfects.

    can alter the protein folding, stability and active site

  • 17

    Which of the ff prosthetic groups is tightly bound to the enzyme andis involved in electron transfer

    heme

  • 18

    Whichof the ff enzymes exhibits multiclas functionality

    alcohhol dehydrogenase

  • 19

    Which of the ff is NOT common characteristic of competative inhibation

    the inhibitor binds irreversibly to the enzyme

  • 20

    Which of the ff types of immune cells recognize specific amino acid sequence on antigens

    t cells

  • 21

    Single amino acid substitution in hemoglobin can cause sickle cell anemia due to

    change in tertiart structure of hemoglobin

  • 22

    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

  • 23

    Which of the ff statements is true regardig Flavin Mononucleotide (FMN) and Flavin Adenine Dinucleotide

    both FMN and FAD contains flavin ring structure

  • 24

    Techniques relies on the cleavage of peptide bonds at specific amino acids residue to determine the amino acid sequence

    mass spectoscopy

  • 25

    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

  • 26

    Which tf the ff statement describes the role of peptide bonds protein structure

    link amio acid together to form polypeptide chain

  • 27

    Which of the ff essential amino avid plays a crucial role in the synthesis of neurotransmitters like serotonin and melatonin

    tryptophan

  • 28

    Which of the ff metabolic processes directly utilizes S-adenosylmethionine (SAM) as methyl donor

    DNA methylation

  • 29

    Which technique can be used to study the kinetic of peptide bondformation

    stopped flow spect

  • 30

    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

  • 31

    Which of the ff coenzymes is essential in the transfer of one carbon units during metabolic rxn.

    NAD+

  • 32

    A singlle amino acid substitution in a protein can impact stability what factor can contribute to this

    all of the above

  • 33

    Which of the ff is NOT a common characteristics of competitive inhibation

    the inhibitor binds irreversibly to the enzyme

  • 34

    NOT typically lead to protein denaturation

    high substrate conc.

  • 35

    forces primarily drives protein folding

    hydrophobic interactions

  • 36

    Whichh of the ff is correct EC(enzyme commission) number classification for oxireductase

    EC 1

  • 37

    Which isoenzyme pair is clinically significant for diagnosing myocardinal infarction

    LDH 1 and LDH 5

  • 38

    Which level of protein structure s primarily determined by hydrogen bonding between the amide and carbonyl

    secondary struct

  • 39

    Which of the ff bioinformatic tools is commonlu used to predict secondary structure of protein

    PSIPRED

  • 40

    How can the study of conserved peptide motifs help in understandingprotein evolution function

    all of the above

  • 41

    Which of the ff enzymes is classified as a hydrolase

    amylase

  • 42

    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

  • 43

    In the dairy industry, which enzyme is primarily used to curdle milk and separate curds from whey during cheese production

    rennin (chymosin)

  • 44

    Hydrogen bonding pattern in an alpha helix

    four residues away

  • 45

    NOT a common fuction of protein protein interaction

    lipid synthesis

  • 46

    Which type of enzyme inhibation results in a decrease in Vmax but no chage in Km

    competative inhibi

  • 47

    Which metabolic pathway involves the degradation of amino acid to produce energy or to synthesize glucose

    citric acid cycle

  • 48

    How does a competative inhibitor affect the lineweaver burk plot of an enzyme catalyzed rxn

    increases the slope and leaves the y intercept unchanged

  • 49

    Which of the ff is a defining characteristic of prosthetic group compared to coenzyme

    tightly and permanent

  • 50

    Proline residues often disrupts alpha helix because

    lack of hydrogen atom on the alpha amino group

  • 51

    Which of the ff best describes the type of rxn catalyzed by isomerase

    rearrangement of the molecular structure

  • 52

    In a lineweaver burk plot,what does y intercept represent

    inverse of themaximal velocity (1/Vmax)

  • 53

    Which of the ff best describes the effect of an uncompetative inhibator on enzyme kinetics

    Km remains unchanged, Vmax decreases

  • 54

    How does phosphorylation affect enzyme activity in most regulatory enzyme

    can activate or inhibit depending on the enzyme and pathway

  • 55

    Which of the ff information can be directly obtained fron xray crytallography data

    peptide bond angles and bond length

  • 56

    A mutations that alters single amino acid can impact its function. This is primarily due to changes in

    tertiary struct.

  • 57

    NOT a common mechanism employed by chaperones

    directly catalyzing the formation of peptide bonds

  • 58

    Which of the ff is an example of covalent modification regulating enzyme activity

    phosphorylation

  • 59

    Which enzyme can exhibit both transferase and hydrolaase activities depending on the substrate or rxn conditions

    hexokinase

  • 60

    Which rxn is most likely catalyzed by hydrolase

    cleavage of a peptide bond

  • 61

    Which of the ff is the primay goal of Enzyme Replacement Theraphy (ERT)

    replace the deficient or missing enzyme

  • 62

    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

  • 63

    NOT a common mechanism by which enzymes lower activation energy?

    increased substrate conc.

  • 64

    Which of the ff enzymes falls under the category of oxireductases

    lactate dehydrogenase

  • 65

    Deficiency of which essential amino acid can lead to kwashiorkor, severe form of malnutrition characterized by edema, growth retardation and muscle wasting

    threonine

  • 66

    Membrane proteins often adopt complex topologies. What is a common mechanism by which these proteins insert into the lipid bilayer

    chaperone assisted insertion

  • 67

    A protein domain that specifically recognizes and binds to another protein or molecule is known as

    module

  • 68

    A proteins tertiary structure is primarily stabilized by which type of interaction

    hydrogen bonds/hydrophobic interactions/ionic bonds

  • 69

    Which of the ff enzyme defficiencies leads to defect in the synthesis of thyroid hormones, causig a disorder such as congenital hypothyroidism

    5- deiodinase

  • 70

    Which of the ff compounds is synthesized from S- Adenosylmethionine (SAM) through methylation rxn i the body

    acetylcholine

  • 71

    Which of the ff enzyme is commonly used in Enzyme Replacement Theraphy (ERT) to treat Gauchers disease

    imiglucerase

  • 72

    What is the role of chaperones in folding of multidomain protein

    all of the above

  • 73

    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

  • 74

    Which of the ff enzymes is clinically relevant as a biomarker for liver function and is classified under the oxidoreductase enzyme class

    ALT

  • 75

    A defficiency of which essential amino acid can lead to neurological disorder and impaired cognitive function

    tryptophan

  • 76

    Which of the ff is not BCAA?

    threonine

  • 77

    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.

  • 78

    Which of the ff statements best describe isozymes

    enzymes that catalyze the same rxn but differ in their structure and kinetic properties

  • 79

    Which of the ff amino acid is known to introduce flexibility

    glycine

  • 80

    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

  • 81

    Which of the ff essential amino acid has sulfur containing side chaiin

    methionine

  • 82

    Common protein motif in DNA binding

    all of the above

  • 83

    Which of the ff enzymes is classified an an isomerase

    phosphoglucose isomerase

  • 84

    Spectroscopic technique can be used to directly observed the vibrational modes of peptide bonds

    IR spectroscopy

  • 85

    Which of the ff is an example of prosthetic group that participate in electron transfer

    heme

  • 86

    describes the role of disulfide bonds in protein structure

    contribute to the tertiary structure of proteins

  • 87

    Which amino acid is a precursor for the synthesis of heme

    glycine

  • 88

    Which of the ff informations can be obtained from CD spectroscopy

    secondary struct

  • 89

    NOT a common type of interaction in protein binding

    covalent bond

  • 90

    NOT a common mechanism employed by Chaperone

    directly catalyzing peptide bonds

  • 91

    Which of the ff types of missense mutations s most likely to have impact in protein funtion

    non consevative substitution

  • 92

    Which of the ff statements about isopeptide bond is correct

    ormeed between the side chains of amino acid

  • 93

    Which of the ff enzymatic rxn involves biotin as prosthetic group

    carboxylation of pyruvate to form oxaloacetate

  • 94

    Peptide bonds directly participate in which of thee ff types of protein protein interactions

    covalent bonding

  • 95

    Which enzyme is most commonly used in the industrial production of high fructose corn syrup

    isomerases

  • 96

    Which of the ff best describes role of an allosteric activator in enzyme kinetics

    increases substrate binding

  • 97

    Accurately describes the relationship between protein sequence and function

    the amino acid sequence determines its 3D structure, which in turn determines its function

  • 98

    NOT a common post transitional modification that can affect protein function

    replication

  • 99

    Factor that can influence the stability of an alpha helix

    all of the above