19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid an...
1. What amino acids do the following abbreviations stand for? Draw the structure of each. a) lle b) Thr c) Gin 2. Name and draw the structures of the amino acids that fit these descriptions: a) Contains an isopropyl group b) Contains a secondary alcohol group 3. Which of the following objects is chiral? a) A pair of scissors b) A comb c) A drinking glass 4. What does the term achiral mean? Give two examples involving organic structures.. 5....
True or False: The form of dipeptide aspartylserine (Asp-Ser) obtained from two amino acids are drawn as: The form of dipeptide aspartylserine (Asp-Ser) obtained from two amino acids are drawn as:
Choose the amino acids from the list below that could combine to give the following dipeptide. H2-CH- CH-C -OH H CH2 H N—C—C—OH CH2 H N—C—C- -OH CH2 CH2 CH2 CH2 NH2 H2N-CH-C-OH CH2 OH H2N-CH- -C- -OH Н. OO H2N-CH-C-OH CH-CH, сн.
Identify the structural components of an amino acid and understand the chemical diversity of amino acids Question Coo- Anch H₂N-CH2 H2C CH Proline Proline's structure has a unique feature not found in other amino acids. What is it? Select the correct answer below: O Proline is chiral. O The amino group is part of the side chain. O Proline is positively charged. O Proline is achiral. P FEEDBACK MORE INSTRUCTION SUBMIT Content attribution Understand protonation and deprotonation of carboxyl and...
4. Write out the 10 structure for the following polypeptide: он он HyN-CH-C-N-CH-C-N-CH-COO CH2 CH-OH CH C-NH2 CH3 COO 5. Illustrate the possible 2° structure interactions in the following polypeptide: R. 6. Identify the type of 3° structure interaction that will occur between the following pairs of amino acids: a) Aspartic acid and lysine b) Serine and tyrosine c) Leucine and valine d) Cysteine and cysteine 7. Draw out the products of the hydrolysis of the following polypeptide: HsN CH-C-N-C-C-N-C-C-N-CH-C-N-CH-COo...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...
b) Show the dipeptide formed by the following two amino acids: + H₂N-CH-Coo- H₂N-CH-COo + + H₂N CH₂ 1 CH₂ 1 SH Phenylalanine Cysteine eys Phe
Which of the following amino acids has a side chain with an ionizable proton and can exist in four different forms, depending on the pH of the solution? H I. Proine CO IV. Alanine CH-d-cool Η'ΦΗ NH3 N H H II. Serie HO-CH2-c-coo NH V. Glycine H-d-cooo NH HN H IIL Histidine -CH2-Ć-COOB H NH 11 С СО СО IV v Submit Request Answer
On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups. Select one: a. +2 b. -2 c. 0 d. -1 e. +1
The primary structure of a protein is formed by the condensation of amino acids in a certain sequence. Consider the dipeptide formed by the condensation of glycine and tyrosine in Figure 8.31B. a. Draw the structure of the dipeptide that would be formed if the two amino acids condensed in the opposite sequence. b. How are the structures of the dipeptides in Figure 8.31B and your drawing related to each other? B 0 HN-C-0--OH HO H-N-C-C-OH H CHE H OH...