Using the standard 3.6 amino acids per turn (360°) and the helical wheel below, plot each sequence on a helical wheel. Circle the hydrophobic residues and draw a square around the hydrophilic residues. Clearly indicate which of the 4 sequences creates an amphipathic helix where one side is buried on the inside of the protein and the other is exposed to water. Explain why the peptide you chose is the correct one and why the other 3 are incorrect.

Using the standard 3.6 amino acids per turn (360°) and the helical wheel below, plot each sequence on a helical wheel. Circle the hydrophobic residues and draw a square around the hydrophilic residues. Clearly indicate which of the 4 sequences creates an amphipathic helix where one side is buried on the inside of the protein and the other is exposed to water. Explain why the peptide you chose is the correct one and why the other 3 are incorrect.

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter8: The Structure, Replication, And Chromosomal Organization Of Dna

Section: Chapter Questions

Problem 15QP: Using Figures 8.7 and 8.9 as a guide, draw a dinucleotide composed of C and A. Next to this, draw...

See similar textbooks

Similar questions

6) Proline is not commonly found in the middle of a-helices because its ring structure prevents it from adopting the proper value and because it disrupts the hydrogen-bonding pattern of the helix. Looking at the structure of proline in the amino acid sequence below, suggest how this residue would disrupt the hydrogen-bonding pattern of an a-helix. 'N H R N N H *** R
4. A polypeptide comprised of 17 amino acid res- idues with the sequence on the right is ob-served by spectroscopic methods to undergo transitions from an a-helix conformation to a B-sheet as a function of pH and concentration. The acetyl and carboxamide groups are attached covalently to deri- vatize the N- and C-terminal residues, respectively, to avoid charge effects of the end groups. CH3CO-ΤAΤΚΑE LLAKYEATΗK-CONH2 (a) ( amino acid residues. Write the sequence of this polypeptide with corresponding 3-letter abbreviations for the (b) At pH < 4 the polypeptide forms an a-helix. (i) ( the helix? and (ii) (: · with respect to the positive and negative ends of the macrodipole? ) What is the direction of the macrodipole of | Are the charges on the N- and C-terminal residues stabilizing or de-stabilizing (c) (* stabilize the helical conformation. What are the most likely protonation states of the side-chains that provide a-helix stabilizing interactions? Use the helical wheel (at the back…
1. What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. 2. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-
4. Do the "Bond X" bonds in Figure 4 involve atoms in the amino acid R groups or in the polypeptide "backbone"/ "main chain" atoms? 5. Given Your Answer To “b," are each of the following statements True or False? Be able to explain your reasoning. o Only very specific primary sequences can form a-helices and B-sheets. o Many different primary sequences can form a-helices and B-sheets. Each arrow depicted in Figure 4D represents consecutive amino acids in the primary sequence of the polypeptide, while the different arrows may be formed from amino acids that are removed from each other in the primary sequence. Each arrow is referred to as a B-strand, and the structure formed through interaction of the B-strands is the B-sheet. In a complete protein, other segments of the protein would connect the different B-strands. 6. Do the "Bond X" bonds in the B-sheet connect atoms from the same B-strand or neighboring strands? TERTIARY STRUCTURE (A) (B) (C) Figure 4-17 Essential Cell Biology 3/e (o…
1. If you were to write the amino acid sequence of the polypeptide segment using one-letter abbreviations, the first two letters in the sequence would be ___. Note: For the tripeptide valylglycyltryptophan, its sequence in one-letter abbreviations will be written as VGW.Choices: EA DA AG AH GA 2. If this segment were to form an ?α-helix, the oxygen atom inside the red box will hydrogen bond with which of the indicated atoms? Write the letter pointing to the atom. [hbond_partner]Choices: A B C D E F
3. The primary amino acid sequence of a stretch of polypeptide is Asp-Glu-Pro- Lys-His-Arg. Would you expect this portion of the polypeptide to form an alpha helix at PH35? Provide 3 reasons to justify your answer.
4. A polypeptide comprised of 17 amino acid res- idues with the sequence on the right is ob-served by spectroscopic methods to undergo transitions from an a-helix conformation to a B-sheet as a function of pH and concentration. The acetyl and carboxamide groups are attached covalently to deri- vatize the N- and C-terminal residues, respectively, to avoid charge effects of the end groups. CH3CO-ETATKAELLAKYEATHK-CONH2 (а) amino acid residues. Write the sequence of this polypeptide with corresponding 3-letter abbreviations for the (b) At pH < 4 the polypeptide forms an a-helix. (i) the helix? and (ii) with respect to the positive and negative ends of the macrodipole? What is the direction of the macrodipole of Are the charges on the N- and C-terminal residues stabilizing or de-stabilizing
1.Draw these phosphorylated structures as they would be connected in a polinucleotide (e.g.RNA) in the order A-B. / Show how they combine to form the polynuleotide (i.e. only the end product). Show at any one of these structures where the glycosidic bond occurs 2.Sanger sequencing revealed the sequence of an oligonucleotide to be: d-AGATGCCTGACT. Draw a diagram of the gel banding pattern post capillary electrophoresis i.e. where on the gel would the fragments feature
Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix
In the given structure below, 1. What protein was used as the template for modelling the structure of the assigned amino acid sequence? 2. How many alpha-helices and beta-sheets are there?
An a helix would be destabilized MOST by ○ a glycine residue adopting alpha-helical backbone dihedral angles ○ interactions between neighboring Asp and Arg residues ○ interactions between two adjacent hydrophobic Val residues O the presence of an Arg residue near the carboxyl terminus of the a helix O the presence of two Lys residues near the amino terminus of the a helix
Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Gly , Ser, Thr, Cys, Tyr, Asn Gln Phe: F Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle: I Trp: W Туr: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense