1. Draw the dipeptide His-Gly at pH 7.4. 2. Label the amino terminus, the carboxy terminus, the two alpha carbons, and the peptide bond (1pt). 3. Calculate it’s net charge. 4. What is the net charge of this dipeptide at pH = 2? 5. List the levels of protein structure and the types of bonds/interactions that are characteristic of each level.
1. Draw the dipeptide His-Gly at pH 7.4. 2. Label the amino terminus, the carboxy terminus,...
Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the following: a) Peptide bond b) N-terminus c) C-terminus d) An α-amino group and an ε-amino group e) An α-carboxylate group and a Y-carboxylate group Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the following: (a). peptide bond, (b). N-terminus, (c). C-terminus, (d). an a-amino group and an e-amino group, (e), an α-carboxylate group and a -carboxylate group.
Can anyone confirm if these are correct? List and draw the structure(s) the amino acid(s) in which would have a-1 net charge at pH? List the amino acid(s) in which would have a + 1 net charge at pH 7? Draw the structure- of the peptide Arg-Asp-His-Ser-Gly at pH 7. List the N-terminus and C-terminus. Make sure the amide bonds are 'trans'. Give the products of a trypsin digestion of the peptide: His-phe-lys-val-asp-asp-arg-val Draw the full structure of the predominant...
9 (a) In the box below, draw the dipeptide Phe-Arg at pH 7, with the N-terminus at the left and the C-terminus on the right. 9 (b) Draw a single box around the three non-hydrogen atoms directly involved in the peptide bond. 9 (c) Label the Phi (φ) and Psi (ψ) torsion angles in your drawing. 9 (d) How many positive charges are on this dipeptide at pH 7? 9 (e) What is the total net charge at pH 7...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptide that forms between serine and alanine. The dipeptide sequence is Ser-Ala. Label the peptide bond. 3.) How many amino acids residues are in a polypeptide containing 6 peptide bonds? How many peptide bonds are in a tripeptide 4.) Sketch a alpha-helix and a beta-sheet as best as you can. Label each.
1. What is the name for the dipeptide shown below 2. Label each as primary, secondary, tertiary, or quaternary 3. Indicate whether each is hydrophobic or hydrophilic: Ananine, Tyr, Lysine, V CH, O CH OH NH-CH=C-NHCHCOOH The protein folds into a compact structure stabilized by interactions between R groups. the combination of two or more protein molecules to form an active protein pleated sheet the peptide bonds between the amino acids the structural level achieved when hydrogen bonds form between...
PRELAB ASSIGNMENT 1 Draw the structure of the amino acid son CH-OH Label the alpha carbon acid Sorine (en) which has R MO CHE OH CH2 OH 2. Draw the dipeptide that forms betw the peptide bond. s between serine and alanine The dipeptide sequence is Ser Ala Lace CH NCH H, A - — сH — с CH2 OH 3. How many amino aci arty amino acid residues are in a polypeptide containing 6 peptide bonos How many peptide...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid and serine, whose structures are shown here, is HiN-CH-C-0HIN-CH-C-0 CH2 CH OH aspartic acid serine A HN-CH-C-o-N-CH-C-o CH OH CH2 coo -(H-C-o-H-c-o CH OH CH2 HIN CH-C-N-CH-C-O CH OH CH H-CH-CH CH CH OH coo- 20) Where is the peptide bond located in this dipeptide? serine valine a) the CO-NH joining serine and the valine b) the doubly bonded oxygen just left of center between the...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
Biochem help 2 14. What would be the net charge on the dipeptide Ser-His at pH- 6.04? (Choose the one best answer.) a) 1.5 b) +1; c) +0.5 d) 0 e) -0.5; 15. The pKa of a lysine side chain in a protein ending up on the outside of a globular protein has a different pKa than if the lysine is buried within the interior of a protein. What would be the expected pKa of a side chain of lysine...