1. An HEXAPEPTIDE was sequenced using differing enzyme and chemical reagents. The results of these experiments, along with an explanation of how to interpret the results, are provided below. Using this information, provide the 1˚ structure for this HEXAPEPTIDE. For the answer, be sure to include the following:
A. Work/answers for Points B-F.
B. The final sequence using 1 letter abbreviations for each amino acid.
C. The structure of the final peptide drawn in MarvinSketch.
Results from Sequencing Experiments on the HEXAPEPTIDE
A. The amino acid content in the peptide was: Y, R, M, K, G, D
B. Reactions with the peptide and 1-fluoro-2,4-dinitrobenzene yielded DNP-G.
C. Treatment of the peptide with chymotrypsin yielded two tripeptides.
D. Treatment of the peptide with trypsin yielded three dipeptides.
E. Treatment of the peptide with carboxypeptidase yielded methionine.
F. N-terminal sequencing of one the chymotrypsin-produced tripeptides (from part C) yielded DNP-K.
1. An HEXAPEPTIDE was sequenced using differing enzyme and chemical reagents. The results of these experiments,...
2. (7 pts) What is the sequence of the following HEXAPEPTIDE? *PROVIDE WORK/ANSWER for B-F! (Use deductive reasoning) Observations from Sequencing Experiments: A. The Sequence contains the following amino acids: Y, R, M, K, G,D B. Reaction with 1-fluoro-2,4-dinitrobenzene yielded DNP-G. C. Treatment with chymotrypsin yielded two tripeptides. D. Treatment with trypsin yielded three dipeptides. E. Treatment with carboxypeptidase yielded methionine. F. N-terminal sequencing of one of the chymotrypsin-produced tripeptides yielded DNP-K Explanation and summary of protein sequencing techniques •...
(7 pts) What is the sequence of the following HEXAPEPTIDE? *PROVIDE WORK/ANSWER for B-F! (Use deductive reasoning) Observations from Sequencing Experiments: A. The Sequence contains the following amino acids: Y, R, M, K, G, D B. Reaction with 1-fluoro-2,4-dinitrobenzene yielded DNP-G. ___ ___ ___ ____ ___ ___ y = 0.058x + 0.0081 y = 0.2711x + 0.0105 -0.02 0 0.02 0.04 0.06 0.08 0.1 0.12 0.14 -0.2 -0.1 0 0.1 0.2 0.3 0.4 0.5 Velocity ( mM/min) -1 [S] mM-1...
1. Partial hydrolysis of lysozyme yielded an octapeptide that was later identified as the N-terminal segment of the protein. From the following information, determine the sequence of this octapeptide. a. The following amino acids were identified after complete hydrolysis of the octapeptide: Arginine (Arg) Glycine (Gly) Phenylalanine (Phe) Cysteine (Cys) Leucine (Leu) Valine (Val) Glutamic Acid (Glu) Lysine (Lys) b. Treatment of the octapeptide with dinitroflurobenzene (Sanger reagent) followed by complete hydrolysis gave lysine (Lys) labeled with two dinitrophenyl (DNP) groups. c. Treatment of the octapeptide with trypsin gave lysine...
1. Partial hydrolysis of lysozyme yielded an octapeptide that was later identified as the N-terminal segment of the protein. From the following information, determine the sequence of this octapeptide. a. The following amino acids were identified after complete hydrolysis of the octapeptide: Arginine (Arg) Glycine (Gly) Phenylalanine (Phe) Cysteine (Cys) Leucine (Leu) Valine (Val) Glutamic Acid (Glu) Lysine (Lys) b. Treatment of the octapeptide with dinitroflurobenzene (Sanger reagent) followed by complete hydrolysis gave lysine (Lys) labeled with two dinitrophenyl (DNP) groups. c. Treatment of the octapeptide with trypsin gave lysine...
A chain GIVEQCCASVCSLYQLENYCN B chain FVNQHLCGSHLVEALYLVCGERGFFYTPKA Shown above is the amino acid sequence of the hormone insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. When Sanger and colleagues began their work in 1945, it was known that insulin was a small protein consisting of two or four polypeptide chains linked by disulfide bonds. Sanger and his coworkers...
15,16,17
15 Thermodynamic parameters (entropy, enthalpy free energy, and internal energy) are given for an unknown chryme Explain which results would be expected for the breaking of hydrogen bonds and the exposure of hydrophobie groups from the interior during the unfolding process of a protein. B1 A B. C. D. E. Entropy change, AS, is zero. Enthalpy change, AH, is positive. The reaction is spontaneous. Enthalpy change, AH, is negative. Entropy change, AS, is positive. Insulin is a polypeptide hormone...
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...