Homework Answers
Chymotripsin is a collection of three amino acids called catalytic triad.This triad consists of a serine -195,histidine -57 and aspartate -102.These amino acids work together to carry out the catalytic function of breaking peptide bonds.The side chain of serine is bonded to the imidazole ring of the histidine residue which accepts a proton from serine to form a strong alkoxide nucleophile in the presence of a substrate for attack.The histidine residue forces serine into a position that facilitates nucleophilic attack later on through the process of catalysis by approximation.
The histidine was in the position to act as a base, a proton acceptor, and remove the proton from the OH group of serine. With this change , the serine is much more reactive, and can easily form a new bond with the carbon atom in the peptide bond of the substrate.
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6. For serine to work effectively as a nucleophile in covalent catalysis in chymotrypsin a nearby...
Identify the kind of chemical catalysis and then identify which of the given amino acids can...
Identify the kind of chemical catalysis and then identify which of the given amino acids can act as a catalyst for the reaction. HN-C-Coo H ¢-Coo HN— _—-coo MN -COOHN- -c coo histidine glutamic acid serine methionine lysine O că-oá D D HOH glutamic acid serine lysine histidine methionine caro Сх OH , Which amino acid would catalyze the reaction? The reaction is an example of acid-base catalysis covalent catalysis O glutamic acid O serine lysine histidine O methionine metal...
Chymotrypsin What evidence in chymotrypsin mechanism supports the claim that chymotrypsin catalysis involves general acid-base catalysis...
Chymotrypsin What evidence in chymotrypsin mechanism supports the claim that chymotrypsin catalysis involves general acid-base catalysis and covalent catalysis? Draw the chemical structure of the transition state (resembles the intermediate structure) in the step that forms the enzyme-product covalent adduct. In comparison to the substrate, how is the tetrahedral transition state preferentially stabilized by enzyme? Chymotrypsin mechanism: Write all the steps in the mechanism and understand what each step accomplishes.
Are the following examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or...
Are the following examples of general acid/base catalysis, covalent
catalysis, catalysis by approximation (proximity effect), or
metal-ion catalysis? Complete parts a, b, c, and d.
(b) NMP kinases bring two nucleotides, for example AMP and ATP,
together to facilitate the transfer of a phosphoryl group from one
nucleotide to the other (creating two ADP). The enzyme positions
the adenosine triphosphate (ATP) such that the gamma phosphate
group is placed adjacently to the phosphate group of the NMP
kinase. This facilitates...
The HIV protease enzyme uses a general acid-base catalysis mechanism to cleave viral polypeptides but does...
The HIV protease enzyme uses a general acid-base catalysis mechanism to cleave viral polypeptides but does not use a covalent catalysis. This enzyme functions optimally in the pH range of 4-6. Due to the specific amino acids involved in this catalysis, HIV protease is a member of which subclass of proteases? Select one: A. metalloproteases B. aspartyl proteases C. serine proteases D. lysine proteases E. cysteine proteases
The following 6 steps occur in the serine protease mechanism. A. C-O bond breaks B. Histidine...
The following 6 steps occur in the serine protease mechanism. A. C-O bond breaks B. Histidine acts as a general acid to substrate N atom. C. Histidine acts as a general base to H2O. D. N-C covalent bond breaks. E. Serine acts as a general acid. F. Serine acts as general base. Put the following into the correct chronological order (as follows: ABCDEF)
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
C3) (5 points) a) Explain (in words) how it is chemically possible for His57 to deprotonate...
C3) (5 points) a) Explain (in words) how it is chemically possible for His57 to deprotonate the sidechain hydroxyl of Ser195 during chymotrypsin catalysis, when a standard histidine sidechain has a pk, of 6. Be specific. b) Bacterial type I signal peptidase is also in the serine protease family of enzymes. However, rather than histidine, this enzyme has lysine in its place (adjacent to the serine in the active site). What unusual property must this lysine sidechain have in order...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at pH-4 suggests the involvement of an catalytic step Question 8 (1 point) Cellulose and glycogen are both structural polysaccharides proton donation that is mediated by a coenzyme True False free proton surrounded by a hydrophobic environment proton transfer with a pK close to 4 Question 9 (1 point) proton abstraction that requires a metal ion in close proximity The activity of lysozyme is greater...
Covalent and non-covalent bonds. Hydrogen bonds: what type of interaction, which atoms are involved. Covalent bonds,...
Covalent and non-covalent bonds. Hydrogen bonds: what type of interaction, which atoms are involved. Covalent bonds, hydrogen bonds, Van der Waals forces, electrostatic interactions. Polarity of water What is the maximum number of hydrogen bonds that one water molecule can have with neighboring water molecules? Hydrophobic and hydrophilic molecules. Colligative properties of water Osmosis: water flow Isotonic, hypertonic and hypotonic cells: describe Amphipathic molecules. What is the molecular structure of water? Water as a universal solvent Define and describe cohesion...
Can someone please help with questions 14, 16,& 20 Name two sulfur amino acids. IgG. IgA...
Can someone please help with questions 14, 16,& 20
Name two sulfur amino acids. IgG. IgA and IgM antibodies are proteins that arc stabilized by disulfide bonds. Explain the formation of this type of bond and the type. Explain one of the posttranslational modification that happens to collagen. Deficiency of Vitamin C (ascorbate) can cause Scurvy. Explain the mechanism. D-serine is a neurotransmitter. Explain the stereochemistry and the enzymatic conversion of substrate into product. Methionine can also be classified as...
Identify the kind of chemical catalysis and then identify which of the given amino acids can act as a catalyst for the reaction. HN-C-Coo H ¢-Coo HN— _—-coo MN -COOHN- -c coo histidine glutamic acid serine methionine lysine O că-oá D D HOH glutamic acid serine lysine histidine methionine caro Сх OH , Which amino acid would catalyze the reaction? The reaction is an example of acid-base catalysis covalent catalysis O glutamic acid O serine lysine histidine O methionine metal...
Are the following examples of general acid/base catalysis, covalent
catalysis, catalysis by approximation (proximity effect), or
metal-ion catalysis? Complete parts a, b, c, and d.
(b) NMP kinases bring two nucleotides, for example AMP and ATP,
together to facilitate the transfer of a phosphoryl group from one
nucleotide to the other (creating two ADP). The enzyme positions
the adenosine triphosphate (ATP) such that the gamma phosphate
group is placed adjacently to the phosphate group of the NMP
kinase. This facilitates...
The HIV protease enzyme uses a general acid-base catalysis mechanism to cleave viral polypeptides but does not use a covalent catalysis. This enzyme functions optimally in the pH range of 4-6. Due to the specific amino acids involved in this catalysis, HIV protease is a member of which subclass of proteases? Select one: A. metalloproteases B. aspartyl proteases C. serine proteases D. lysine proteases E. cysteine proteases
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
C3) (5 points) a) Explain (in words) how it is chemically possible for His57 to deprotonate the sidechain hydroxyl of Ser195 during chymotrypsin catalysis, when a standard histidine sidechain has a pk, of 6. Be specific. b) Bacterial type I signal peptidase is also in the serine protease family of enzymes. However, rather than histidine, this enzyme has lysine in its place (adjacent to the serine in the active site). What unusual property must this lysine sidechain have in order...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at pH-4 suggests the involvement of an catalytic step Question 8 (1 point) Cellulose and glycogen are both structural polysaccharides proton donation that is mediated by a coenzyme True False free proton surrounded by a hydrophobic environment proton transfer with a pK close to 4 Question 9 (1 point) proton abstraction that requires a metal ion in close proximity The activity of lysozyme is greater...
Can someone please help with questions 14, 16,& 20
Name two sulfur amino acids. IgG. IgA and IgM antibodies are proteins that arc stabilized by disulfide bonds. Explain the formation of this type of bond and the type. Explain one of the posttranslational modification that happens to collagen. Deficiency of Vitamin C (ascorbate) can cause Scurvy. Explain the mechanism. D-serine is a neurotransmitter. Explain the stereochemistry and the enzymatic conversion of substrate into product. Methionine can also be classified as...
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