biochem

99問 • 1年前

velante

通報

問題一覧

describes the role of disulfide bonds in protein structure

contribute to the tertiary structure of proteins

NOT a common mechanism employed by chaperones

directly catalyzing the formation of peptide bonds

forces primarily drives protein folding

hydrophobic interactions

Mutation that disrupts disulfide bond that lead to loss of function

loss of tertiay structure stability

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

change in tertiart structure of hemoglobin

Which of the ff statements about PROTEIN DOMAINS is FALSE

always encoded by single exon

Hydrogen bonding pattern in an alpha helix

four residues away

Proline residues often disrupts alpha helix because

lack of hydrogen atom on the alpha amino group

NOT a common type of interaction in protein binding

covalent bond

NOT affect the BINDING AFFINITY

genetic code

Common protein motif in DNA binding

all of the above

NOT a common mechanism by which enzymes lower activation energy?

increased substrate conc.

Which of the following statement is correct about PHENYLALANINE

remains essential amino acid

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

tertiary struct.

NOT a common post transitional modification that can affect protein function

replication

NOT a common mechanism employed by Chaperone

directly catalyzing peptide bonds

NOT typically lead to protein denaturation

high substrate conc.

Accurately describes the relationship between protein sequence and function

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

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

can alter the protein folding, stability and active site

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.

Factor that can influence the stability of an alpha helix

all of the above

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

module

NOT a common fuction of protein protein interaction

lipid synthesis

Which of the following statements about protein domain is FALSE

always encoded by single exon

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

the inhibitor binds irreversibly to the enzyme

Which of the ff is NOT common characteristic of competative inhibation

the inhibitor binds irreversibly to the enzyme

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

tryptophan

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

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

citric acid cycle

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

threonine

Which of the ff is not BCAA?

threonine

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

link amio acid together to form polypeptide chain

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

covalent bonding

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

mass spectoscopy

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

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

IR spectroscopy

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

all of the above

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

non consevative substitution

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

PSIPRED

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

t cells

Which of the ff amino acid is known to introduce flexibility

glycine

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

secondary struct

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

methionine

Which amino acid is a precursor for the synthesis of heme

glycine

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

enhanced cognitive function

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

tryptophan

Which of the ff statements about isopeptide bond is correct

ormeed between the side chains of amino acid

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

peptide bond angles and bond length

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

all of the above

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

stopped flow spect

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

alanine to proline

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

all of the above

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

Why are ceertain amino acid sequences more immunogenic than others

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

Howcan amino acid sequence influence the conformational flexibility of a protein

alll of the above

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

hydrogen bonds/hydrophobic interactions/ionic bonds

Which of the ff informations can be obtained from CD spectroscopy

secondary struct

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

solid state NMR spect

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

each domain folds independently

Which of the ff enzymes falls under the category of oxireductases

lactate dehydrogenase

Which of the ff enzymes is classified as a hydrolase

amylase

Which of the ff enzymes is classified an an isomerase

phosphoglucose isomerase

Whichof the ff enzymes exhibits multiclas functionality

alcohhol dehydrogenase

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

ALT

In a lineweaver burk plot,what does y intercept represent

inverse of themaximal velocity (1/Vmax)

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

competative inhibi

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

increases substrate binding

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

phosphorylation

Which isoenzyme pair is clinically significant for diagnosing myocardinal infarction

LDH 1 and LDH 5

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

NAD+

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

DNA methylation

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

tightly and permanent

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

preventing protein aggregation

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

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

chaperone assisted insertion

What is the role of chaperones in folding of multidomain protein

all of the above

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

EC 1

Which rxn is most likely catalyzed by hydrolase

cleavage of a peptide bond

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

rearrangement of the molecular structure

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

hexokinase

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

isomerases

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

increases the slope and leaves the y intercept unchanged

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

Km remains unchanged, Vmax decreases

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

How does phosphorylation affect enzyme activity in most regulatory enzyme

can activate or inhibit depending on the enzyme and pathway

Which of the ff statements best describe isozymes

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

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

heme

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

acetylcholine

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

heme

Which of the ff enzymatic rxn involves biotin as prosthetic group

carboxylation of pyruvate to form oxaloacetate

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

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

replace the deficient or missing enzyme

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

amylase

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

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

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

both FMN and FAD contains flavin ring structure

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

imiglucerase

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

rennin (chymosin)

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

5- deiodinase

inorg

inorg

phychem

phychem

GREAT BOOKS

velante · 56問 · 10ヶ月前

GREAT BOOKS

56問 • 10ヶ月前

velante

BIOCHEMZ (bioenergetics)

velante · 12問 · 10ヶ月前

BIOCHEMZ (bioenergetics)

12問 • 10ヶ月前

velante

BIOCHEMZ (cellular respi.)

velante · 28問 · 10ヶ月前

BIOCHEMZ (cellular respi.)

28問 • 10ヶ月前

velante

BIOCHEMZ(glycolysis)

velante · 28問 · 10ヶ月前

BIOCHEMZ(glycolysis)

28問 • 10ヶ月前

velante

BIOCHEMZ(fates of pyruv)

velante · 33問 · 10ヶ月前

BIOCHEMZ(fates of pyruv)

33問 • 10ヶ月前

velante

BIOCHEMZ(krebs)

velante · 32問 · 10ヶ月前

BIOCHEMZ(krebs)

32問 • 10ヶ月前

velante

BIOCHEMZ(ETC)

velante · 47問 · 10ヶ月前

BIOCHEMZ(ETC)

PHYCHEM

PHYCHEM

PHYCHEM 2

PHYCHEM 2

FOOD CHEM food quali

FOOD CHEM food quali

FOOD CHEM water charact

velante · 61問 · 9ヶ月前

FOOD CHEM water charact

FOOD CHEM starch

FOOD CHEM starch

FOOD CHEM starch 2

FOOD CHEM starch 2

FOOD CHEM pectins

FOOD CHEM pectins

ANACHEM m1

ANACHEM m1

ANACHEM m2

ANACHEM m2

ANACHEM m3

ANACHEM m3

問題一覧

describes the role of disulfide bonds in protein structure

contribute to the tertiary structure of proteins

NOT a common mechanism employed by chaperones

directly catalyzing the formation of peptide bonds

forces primarily drives protein folding

hydrophobic interactions

Mutation that disrupts disulfide bond that lead to loss of function

loss of tertiay structure stability

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

change in tertiart structure of hemoglobin

Which of the ff statements about PROTEIN DOMAINS is FALSE

always encoded by single exon

Hydrogen bonding pattern in an alpha helix

four residues away

Proline residues often disrupts alpha helix because

lack of hydrogen atom on the alpha amino group

NOT a common type of interaction in protein binding

covalent bond

NOT affect the BINDING AFFINITY

genetic code

Common protein motif in DNA binding

all of the above

NOT a common mechanism by which enzymes lower activation energy?

increased substrate conc.

Which of the following statement is correct about PHENYLALANINE

remains essential amino acid

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

tertiary struct.

NOT a common post transitional modification that can affect protein function

replication

NOT a common mechanism employed by Chaperone

directly catalyzing peptide bonds

NOT typically lead to protein denaturation

high substrate conc.

Accurately describes the relationship between protein sequence and function

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

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

can alter the protein folding, stability and active site

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.

Factor that can influence the stability of an alpha helix

all of the above

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

module

NOT a common fuction of protein protein interaction

lipid synthesis

Which of the following statements about protein domain is FALSE

always encoded by single exon

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

the inhibitor binds irreversibly to the enzyme

Which of the ff is NOT common characteristic of competative inhibation

the inhibitor binds irreversibly to the enzyme

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

tryptophan

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

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

citric acid cycle

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

threonine

Which of the ff is not BCAA?

threonine

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

link amio acid together to form polypeptide chain

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

covalent bonding

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

mass spectoscopy

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

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

IR spectroscopy

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

all of the above

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

non consevative substitution

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

PSIPRED

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

t cells

Which of the ff amino acid is known to introduce flexibility

glycine

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

secondary struct

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

methionine

Which amino acid is a precursor for the synthesis of heme

glycine

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

enhanced cognitive function

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

tryptophan

Which of the ff statements about isopeptide bond is correct

ormeed between the side chains of amino acid

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

peptide bond angles and bond length

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

all of the above

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

stopped flow spect

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

alanine to proline

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

all of the above

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

Why are ceertain amino acid sequences more immunogenic than others

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

Howcan amino acid sequence influence the conformational flexibility of a protein

alll of the above

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

hydrogen bonds/hydrophobic interactions/ionic bonds

Which of the ff informations can be obtained from CD spectroscopy

secondary struct

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

solid state NMR spect

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

each domain folds independently

Which of the ff enzymes falls under the category of oxireductases

lactate dehydrogenase

Which of the ff enzymes is classified as a hydrolase

amylase

Which of the ff enzymes is classified an an isomerase

phosphoglucose isomerase

Whichof the ff enzymes exhibits multiclas functionality

alcohhol dehydrogenase

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

ALT

In a lineweaver burk plot,what does y intercept represent

inverse of themaximal velocity (1/Vmax)

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

competative inhibi

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

increases substrate binding

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

phosphorylation

Which isoenzyme pair is clinically significant for diagnosing myocardinal infarction

LDH 1 and LDH 5

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

NAD+

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

DNA methylation

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

tightly and permanent

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

preventing protein aggregation

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

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

chaperone assisted insertion

What is the role of chaperones in folding of multidomain protein

all of the above

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

EC 1

Which rxn is most likely catalyzed by hydrolase

cleavage of a peptide bond

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

rearrangement of the molecular structure

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

hexokinase

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

isomerases

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

increases the slope and leaves the y intercept unchanged

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

Km remains unchanged, Vmax decreases

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

How does phosphorylation affect enzyme activity in most regulatory enzyme

can activate or inhibit depending on the enzyme and pathway

Which of the ff statements best describe isozymes

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

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

heme

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

acetylcholine

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

heme

Which of the ff enzymatic rxn involves biotin as prosthetic group

carboxylation of pyruvate to form oxaloacetate

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

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

replace the deficient or missing enzyme

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

amylase

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

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

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

both FMN and FAD contains flavin ring structure

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

imiglucerase

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

rennin (chymosin)

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

5- deiodinase