2) A) Amino acids such as Phe and Val are not known to participate directly in acid-base or coval...
Biochemists oftentimes mutate (change) amino acids in an enzyme in order to learn about their function in catalysis. When one particular Asp residue in Enzyme A was changed (mutated) to an Ala residue, Enzyme A was not able to carry out catalysis (i.e. it became inactive). The most reasonable explanation for this observation is that: This enzyme works through an acid-base mechanism This enzyme works through covalent catalysis Mutation to Ala allows this enzyme to bind metals. This enzyme was...
2. Amino Acids a.) Which amino acid is this: A substitution on the methyl group of this amino acid with a hydroxyl group yields the amino acid Ser and substitution with a phenyl group yields the amino acid Phe. b.) Which amino acid has an a-amino group that is bonded directly to two C atoms, forming a ring?
Explain why amino acid functional groups that participate in acid-base chemistry have perturbed pKa values from simple methyl substituted amino and carboxyl groups. (3 points) Explain why amino acid functional groups that participate in acid-base chemistry have perturbed pKa values from simple methyl substituted amino and carboxyl groups. (3 points)
Question 5 Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
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 activity of many enzymes is regulated by reversible covalent modifications. Kinases add a phosphate group from an ATP to a specific hydroxyl group on an amino acid residue within an enzyme. Which of the following amino acids can be phosphorylated by a kinase? (Select all that apply) Cys His Tyr Thr Phe Ser Val
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...
You have a small gene that encodes the following amino acid: N-MET-ASP-SER-VAL-ALA-ARG-PHE-MET-TRP-C. There is a single mutation in the DNA that causes a change in the amino acid sequence to: N-MET-VAL-GLN-TRP-PRO-ASP-LEU-CYS-GLY-C. a) What kind of mutation is this? Explain. (2 points) b) Indicate the DNA sequence (coding strand) of the gene. Show the original DNA sequence then the mutated sequence. Wild type DNA: Mutant DNA: You have another mutation (a different mutation from the one described in parts a and...
If you have an enzyme that has a primary sequence that is 429 amino acids in length, is it possible that both an amino acid position 215, as well as amino acids located at 342, and 401, can all be part of an active site of a protein? Explain why or why not?
Easy questions, 30 min timed assignment, please answer ASAP thanks. The amino acid least likely to be involved in nucleophilic a. Alanine. b. Asparagine. 1. and/or electrophilic enzyme catalysis is e. All are equally likely c. Aspartate. d. Arginine Fibrous proteins, such as collagen, have which one of the following properties? a. b. c. d. e. 2. highly soluble in water their hydrophilic residues are directed into the interior of the protein exhibits enzymatic activity serve structural roles in the...