Question
please answer

4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Sp
0 0
Add a comment Improve this question Transcribed image text
Answer #1

A helix is formed by interaction between molecules of a protein. These interactions are caused by Hydrogen bonds, vander-vals forces, ionic interactions. All these interactions are non covalent.

a). Given figure has hydrogen bonds indicated by dotted lines. Hydrogen bonds are formed between hydrogen of one molecule and oxygen of another molecule.

b). Hydrogen bonds are non covalent bonds.

c). We already know that, non-covalent bonds are transient. They break easily.

d). Amino acids have a backbone molecule and a side chain. Backbone molecules consists of one amino group bonded with carboxylic group, and side chain consists of long chains denoted by R. It is clear in the figure that, hydrogen bonds are present between backbone molecules of amino acids and not between side chains.

e). As mentioned earlier, amino acid contains one carboxylic group bonded to amino group. Each amino acid has one alpha carbon to which both the groups are bonded, also side chains are bonded to this alpha carbon.

In the figure, the hydrogen bond is present between hydrogen of 1st amino acid and the fourth amino acid molecule.

This means, the interaction is 3 residues away.

f). The side chains are pointing away from the helix. This is the only conformation for thiis alpha helix beacuse, some side chains can be very long. This will create unwanted crowding of molecules if they point inside the helix, hindering the hydrogen bond formation, thus disrupting the formation of alpha helix structure.

Add a comment
Know the answer?
Add Answer to:
please answer 4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2)...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • please answer 5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2)...

    please answer 5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of a B-sheet. The image on the left is of an anti-parallel sheet, and the right of a parallel sheet. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the amino acid (backbone or side chain) are...

  • pls answer 6 and 7 6. Secondary structure (turn): The image below is of a polypeptide...

    pls answer 6 and 7 6. Secondary structure (turn): The image below is of a polypeptide in secondary (20) structure level of protein folding. Specifically it is of a turn. Turns vary in length. The shorter the turn the more drastic the angle changes. The longer the turn, the more gradual the angles needed. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? Is this bond/interaction permanent or transient? d. What parts...

  • please answer 8. Quaternary structure: The image below is of a polypeptide in quaternary (4°) structure...

    please answer 8. Quaternary structure: The image below is of a polypeptide in quaternary (4°) structure level of protein folding. The image to the left is of hemoglobin. It is composed of four separate polypeptide chains indicated by the color differences. The image on the right indicates the backbone items as a ribbon (or line), while the side chains are chemically drawn. a. Name the specific bond/interaction indicated by the: i. Letter A ii. Letter B iii. Letter C iv....

  • Which interaction holds the a-helix and the B-pleated sheet into its unique folding pattern? hydrogen bonding...

    Which interaction holds the a-helix and the B-pleated sheet into its unique folding pattern? hydrogen bonding between nitrogens and oxygens in the polypeptide backbone hydrogen bonding between serines (-CH2OH) covalent bonding between cysteines (-CH2SH) ionic bonding between acidic and basic amino acid side chains hydrophilic interactions

  • What happens when a primary structure forms a secondary structure? Match the words in the left...

    What happens when a primary structure forms a secondary structure? Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer. Terms may be used once, more than once, or not at all. Reset Help carboxylic acid a helix When atoms in the backbone of a protein or peptide form within a single or between chains, a secondary structure results. The two most common...

  • The type of bonding that maintains the secondary structure in a protein is the

    The type of bonding that maintains the secondary structure in a protein is theA) Hydrogen bonds between the carbonyl and amino groups of the backboneB) Covalent bond between the carbonyl and amino groups of the amino acidsC) Hydrogen bonds between two amino acidsD) Disulfide bonds that hold two polypeptide chains togetherE) Hydrogen bonds between two amino groups

  • (1) Describe what you see, using terms that indicate the type of secondary structure shown. (2)...

    (1) Describe what you see, using terms that indicate the type of secondary structure shown. (2) What can you conclude about protein's cellular location from this view of the protei? (3) Why is this amino acid found predominantly on the side of the helices that face each other? (its Leucine) (4) The labels will include the l-letter designation of the amino acid, followed by a number and letter. What does the number indicate? What does the letter indicate? Is this...

  • (2%) Indicate which secondary structure or structures (α -helix, β -pleated, random coil) will the following...

    (2%) Indicate which secondary structure or structures (α -helix, β -pleated, random coil) will the following peptide adopt in an aqueous solution at pH 7 (2%) The unfolding of the alpha helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Glu residues, has the alpha helical conformation at pH 3....

  • 1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative...

    1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative polarity of their side chain. Consider a folded protein in an aqueous environment; where would the hydrophobic amino acids likely be found? -Tucked away in the middle of the folded protein -Randomly distributed throughout the protein -Exposed on the exterior surface of the folded protein 2. All proteins exhibit a primary, secondary, and tertiary structure, but not all proteins exhibit a quaternary structure. Describe...

  • 25. Consider two peptide sequences: LKAENDEAARAMSEA and CRAGGFPWDQPGTSN. Which of the two is more likely to adopt an al...

    25. Consider two peptide sequences: LKAENDEAARAMSEA and CRAGGFPWDQPGTSN. Which of the two is more likely to adopt an alpha-helical structure? Why? 26. A beta strand is a stretch of residues in the extended conformation that can participate in a beta sheet. (In the figure at right, beta strands A and B participate in a two-strand sheet.) What sorts of hydrogen bonds are required for the formation of single beta strands and for the formation of beta sheets? backbone- backbone sidechain...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT