How many hydrogen bonds are found in this region of the secondary structure identified? Keep in mind this is a alpha helix so hydrogen bonding occurs every 4th amino acid residue. It says the answer to this 10. 2 but I don't see how. Could you explain to me how you solve this and why that is the answer? Then, I will rate :)
Homework Answers
in this fig above. Each helix has 5 to 6 turns each turn has near about two hydrogen bonds. So total no. Of hydrogen bonds will be between 10 to 12.and hence the answer 10.2.
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How many hydrogen bonds are found in this region of
the secondary structure identified? Keep in...
Not sure if I answered these correctly... 5. In 20 words or less, how are alpha...
Not sure if I answered these correctly... 5. In 20 words or less, how are alpha helix and beta sheet structures held together? - Hydrogen bonds? 6.Which of the following amino acids would least likely be found in an alpha helix structure of a protein? Phenylalanine, Glycine, Proline or Histidine? I don't understand this question.... Please help :( 7. One of the interactions involved in tertiary structure is ion-ion attraction. Name two amino acids that would interact with each other...
Since the secondary structure of a protein results from hydrogen bonding between components shared by all amino acids
Distinguish between the different levels of protein structure, including primary, secondary, tertiary, and quaternary Question Is the following statement true? If not, explain why not: Since the secondary structure of a protein results from hydrogen bonding between components shared by all amino acids (a hydrogen on an amide N on one amino acid interacts with an oxygen on the carbonyl of another amino acid), the secondary structure does not depend on the specific amino acid groups (the R-groups) in the amino acid chain. Select...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys,...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
Predict how many hydrogen bonds are in the following sequence: LSKAVTFRSDSPGARVELKSPGADFTVN. (Hint: First, assign secondary structure...
Predict how many hydrogen bonds are in the following sequence: LSKAVTFRSDSPGARVELKSPGADFTVN. (Hint: First, assign secondary structure elements; also, do not forget the hydrogen bond that exists in tight (β- or γ-) turns!)
24. How does insulin end up with 2 separate chains when it is produced as one sequence o amino acids. (4 points) 25.What is the difference between the hydrogen bonding which holds the secondary p...
24. How does insulin end up with 2 separate chains when it is produced as one sequence o amino acids. (4 points) 25.What is the difference between the hydrogen bonding which holds the secondary protein structures of and alpha helix and a beta pleated sheet together and the hydrogen bonding that holds the tertiary structure together? (4 points) 26. List the 6 classes of enzymes and describe what types of reactions they catalyze. (3 points per class of enzymes, 18...
Please answer all parts a)-c) thouroughly & clearly. A small generic section of the primary structure...
Please answer all parts a)-c) thouroughly & clearly.
A small generic section of the primary structure of an a helix is given below. ?amino acid1 ?amino acid2 ?amino acid3 ?amino acid4 ?amino acid5 ?amino acid6 ?amino acid7? (a) Which amino acid residue?s backbone forms a hydrogen bond with the backbone of the sixth (6th) residue? Choose the correct residue from the drop-down menu. amino acid Select answer (b) Which of the following peptide segments is most likely to be part...
(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....
please answer 4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2)...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. 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...
(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...
Draw the Lewis structure for hydrogen peroxide, H2O2. Based on this structure, how many polar bonds...
Draw the Lewis structure for hydrogen peroxide, H2O2. Based on this structure, how many polar bonds and non-polar bonds are present? 1 polar bond and 2 non-polar bonds 2 polar bonds and 1 non-polar bond no polar bonds and 3 non-polar bonds 3 polar bonds and no non-polar bonds 2 polar bonds and 2 non-polar bonds
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
24. How does insulin end up with 2 separate chains when it is produced as one sequence o amino acids. (4 points) 25.What is the difference between the hydrogen bonding which holds the secondary protein structures of and alpha helix and a beta pleated sheet together and the hydrogen bonding that holds the tertiary structure together? (4 points) 26. List the 6 classes of enzymes and describe what types of reactions they catalyze. (3 points per class of enzymes, 18...
Please answer all parts a)-c) thouroughly & clearly.
A small generic section of the primary structure of an a helix is given below. ?amino acid1 ?amino acid2 ?amino acid3 ?amino acid4 ?amino acid5 ?amino acid6 ?amino acid7? (a) Which amino acid residue?s backbone forms a hydrogen bond with the backbone of the sixth (6th) residue? Choose the correct residue from the drop-down menu. amino acid Select answer (b) Which of the following peptide segments is most likely to be part...
(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....
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. 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...
(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...
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