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You are studying a protein with a known structure. You decide to mutate the protein and then
study how the structure changes due to the mutation made. You want to determine if overall
surface topology (the shape of the surface of your protein) was affected by the mutation - which
type of protein modeling would be most effective to make this determination? - =spacefill model
NH3+ - =ammonia would be found outside the folded protein
N-terminus - =the first part of the protein that exits the ribosome during protein biosynthesis.
During protein synthesis, the covalent bond between amino acids is formed by the process of -
=condensation, also known as dehydration
You are studying a protein with a known structure. You decide to mutate the protein and then
study how the structure changes due to the mutation made. If you want to determine how
secondary structure specifically changes from the wildtype (unmated) protein as compared to the
mutated protein, which type of modeling would you use? - =ribbon model
What is the difference between a domain and a subunit? - =Domain = independently folded
section of a single polypeptide
Subunit = a single polypeptide in a protein composed of multiple polypeptides, Ex: Antibody
In a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This
would... - =Always change the primary structure of a protein, sometimes affect tertiary structure
and function.
In a structure where a carbon is bound to an uncharged amino group, due to differences in
electronegativity between atoms, the nitrogen is... - =partially negatively charged
C-terminus - =the end of a polypeptide or protein that has a free carboxyl group
,peptide bond - =The chemical bond that forms between the carboxyl group of one amino acid
and the amino group of another amino acid
an R group that could make covalent bonds with other R groups in tertiary and/or quaternary
folding - =SH-CH2-C-H
In a structure where a carbon is bound to an uncharged amino group, due to differences in
electronegativity between atoms, the nitrogen can form... - =Van der Waals interactions
an R group that will make ionic bonds with other R groups in tertiary and/or quaternary folding:
- =NH3-CH2-CH2-CH2-CH2-C
"Proteins can never be chemically modified in more than one way at the same time." - =false
"Allostery is defined as the inhibition of enzymes by binding of molecules in the enzyme's active
site." - =False
Allosteric - =is the regulation of an enzyme by binding an effector molecule at a site other than
the enzyme's active site.
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Changing the free energy of the reactants in the reaction - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Raising the activation energy - =no
, If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Temporarily increasing the temperature surrounding the reaction - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Forming a tight binding interaction with the product - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Stabilizing the transition state - =yes
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
initially forming specific non-covalent bonds with the substrate - =yes
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Changing the Gibbs free energy of the reaction - =no
If a protein completely unfolds, would you expect its solubility in water to change? - =yes
Is the Kd higher for enzyme-substrate or enzyme-product? - =enzyme-product
You are studying a protein with a known structure. You decide to mutate the protein and then
study how the structure changes due to the mutation made. You want to determine if overall
surface topology (the shape of the surface of your protein) was affected by the mutation - which
type of protein modeling would be most effective to make this determination? - =spacefill model
NH3+ - =ammonia would be found outside the folded protein
N-terminus - =the first part of the protein that exits the ribosome during protein biosynthesis.
During protein synthesis, the covalent bond between amino acids is formed by the process of -
=condensation, also known as dehydration
You are studying a protein with a known structure. You decide to mutate the protein and then
study how the structure changes due to the mutation made. If you want to determine how
secondary structure specifically changes from the wildtype (unmated) protein as compared to the
mutated protein, which type of modeling would you use? - =ribbon model
What is the difference between a domain and a subunit? - =Domain = independently folded
section of a single polypeptide
Subunit = a single polypeptide in a protein composed of multiple polypeptides, Ex: Antibody
In a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This
would... - =Always change the primary structure of a protein, sometimes affect tertiary structure
and function.
In a structure where a carbon is bound to an uncharged amino group, due to differences in
electronegativity between atoms, the nitrogen is... - =partially negatively charged
C-terminus - =the end of a polypeptide or protein that has a free carboxyl group
,peptide bond - =The chemical bond that forms between the carboxyl group of one amino acid
and the amino group of another amino acid
an R group that could make covalent bonds with other R groups in tertiary and/or quaternary
folding - =SH-CH2-C-H
In a structure where a carbon is bound to an uncharged amino group, due to differences in
electronegativity between atoms, the nitrogen can form... - =Van der Waals interactions
an R group that will make ionic bonds with other R groups in tertiary and/or quaternary folding:
- =NH3-CH2-CH2-CH2-CH2-C
"Proteins can never be chemically modified in more than one way at the same time." - =false
"Allostery is defined as the inhibition of enzymes by binding of molecules in the enzyme's active
site." - =False
Allosteric - =is the regulation of an enzyme by binding an effector molecule at a site other than
the enzyme's active site.
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Changing the free energy of the reactants in the reaction - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Raising the activation energy - =no
, If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Temporarily increasing the temperature surrounding the reaction - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Forming a tight binding interaction with the product - =no
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Stabilizing the transition state - =yes
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
initially forming specific non-covalent bonds with the substrate - =yes
If you agree that the following statement is a way that enzymes increase rates of chemical
reactions:
Changing the Gibbs free energy of the reaction - =no
If a protein completely unfolds, would you expect its solubility in water to change? - =yes
Is the Kd higher for enzyme-substrate or enzyme-product? - =enzyme-product
