1. Draw the tripeptide: Val-Leu-Met at pH 7 with the N-terminus to the left and C-terminus tothe right. On your drawing, do the following:a. Draw a triangle around the alpha carbons.b. Draw a box around the R-groups.c. Circle the atoms capable of hydrogen bonding.d. Highlight the peptide bond.Mavoy bludy2. What specific atoms in your tripeptide (above) can participate in hydrogen bonding?

Amino acids are the monomers of peptides and they have two functional groups like amino group and…

Answered: 1. Draw the tripeptide: Val-Leu-Met at…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Match the areas of a dipeptide with the labeling number. The N-terminus nitrogen: The C-terminus carbon: The two central (a.) Carbons: and The two side chains: and The peptide bond: between and 2 3 H (N: -C. N- 5 8. H12 CH3 13
Draw the structure of STVWY at pH 13. Connect with an arrow the C=0 of the N- terminal residue to the NH that it would be hydrogen bonded to if the peptide was forming a a-helix?
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
Which of the amino acid side-chains would you expect to be protonated (i.e. has not lost its proton) under neutral pH conditions? Include reasons supporting your prediction.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
1 Draw the following polypeptide: Met- Tyr-Val-Ser-Asn 2A Draw the hydrolysis of a dipeptide consisting of phenylaline and glutamic acid. 2B What are the fuctional group present in the side chains of the amino acids.( phenylalanine and glutamic acid) 2C are the sidechains in part 2B hydrophobic or polar 2D where would you expect to find them ( surface or interior of a protein) ? why ?
Match amino Acid R group characteristics to the biochemical bond it can form. Alanine ◆ Glycine Proline Aspartic Acid Lysine Tryptophan ◆ Methionine Threonine Asparagine Histidine A. Pi-bonding aromatic bonds B. Non-polar, contains a sulfur atom C. Non polar bonds D. Amide group bonds E. Inserts a kink (non-freely rotating bond F. Anionic group donating bonds G. Hydroxy group bonding H. Cationic group with pK = 6.0 I. No-R group - highly flexible J. Cationic group donating bond
Select the properties that apply to the secondary structure alpha helices (select all that apply). U 0 can be Antiparallel can be Parallel are typically right handed are typically left handed obeys n+4 rule are formed by the pattern of hydrogen bonding the backbone makes with itself are formed by the pattern of covalent bonds the backbone makes with itself are formed by the pattern of electrostatic attractions the backbone makes with itself
Tt O 8. What are the driving forces that promotes tertiary -3D and quaternary -4D structure formation of proteins. Provide specific examples of the interactions that drive the formation of 3D and 4D structures?

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