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1. Tosyl-L-phenylalanine chloromethyl ketone (TPCK) is an inhibitor of chymotrypsin that binds in the active site...
N-Tosylamido-L-phenylethyl, also called tosyl phenylalanyl chloromethyl ketone, (TPCK) irreversibly inhibits chymotrypsin, and is used as to...
N-Tosylamido-L-phenylethyl, also called tosyl phenylalanyl chloromethyl ketone, (TPCK) irreversibly inhibits chymotrypsin, and is used as to label the active site histidine residue. The COCH2Cl group is the reactive group that binds to the His residue. Why does chymotrypsin bind TPCK? Trypsin, another serine protease, does not bind TPCK. How could TPCK be modified to enable its recognition by trypsin? Choose the most likely substrate, below.
Which amino acids in chymotrypsin are found in the active site and are participants in substrate...
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...
BIOCHEMISTRY PALA (shown below) binds to the active site of ATCase and is an important probe...
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
Biochemistry. Please answer all completely. 13. Identify the electrophilic center and nucleophile in the below image...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
1. According to the paper, what does lactate dehydrogenase (LDH) do and what does it allow...
1. According to the paper, what does lactate dehydrogenase
(LDH) do and what does it allow to happen within the myofiber? (5
points)
2. According to the paper, what is the major disadvantage of
relying on glycolysis during high-intensity exercise? (5
points)
3. Using Figure 1 in the paper, briefly describe the different
sources of ATP production at 50% versus 90% AND explain whether you
believe this depiction of ATP production applies to a Type IIX
myofiber in a human....
N-Tosylamido-L-phenylethyl, also called tosyl phenylalanyl chloromethyl ketone, (TPCK) irreversibly inhibits chymotrypsin, and is used as to label the active site histidine residue. The COCH2Cl group is the reactive group that binds to the His residue. Why does chymotrypsin bind TPCK? Trypsin, another serine protease, does not bind TPCK. How could TPCK be modified to enable its recognition by trypsin? Choose the most likely substrate, below.
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
1. According to the paper, what does lactate dehydrogenase
(LDH) do and what does it allow to happen within the myofiber? (5
points)
2. According to the paper, what is the major disadvantage of
relying on glycolysis during high-intensity exercise? (5
points)
3. Using Figure 1 in the paper, briefly describe the different
sources of ATP production at 50% versus 90% AND explain whether you
believe this depiction of ATP production applies to a Type IIX
myofiber in a human....
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