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8. (4 pts) What is the name of the specific interaction that occurs in the tertiary...
Name: CHEM 131 3. (8 pts) What type of interaction is expected between the side chains...
Name: CHEM 131 3. (8 pts) What type of interaction is expected between the side chains of the following pairs of amino acids (examples include salt bridges, H-bonding, disulfide bonds and dispersion forces)? Tyrosine and asparagine a) b) Leucine and proline c) two cysteines Give an example of two amino acids that could form a salt bridge (chemical structure or 3 letter d) code) 4. (10 pts) ldentify in which structural feature (1, 2" or 3" structure) of a protein...
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges...
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
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...
What type of covalent bond between amino acid side chains functions in maintaining a polypeptide's specific...
What type of covalent bond between amino acid side chains functions in maintaining a polypeptide's specific tertiary structure? disulfide bond ionic bond hydrogen bond peptide bond hydrophobic interaction
3. Look at your plot of the data. Which of the four reagents was the most effective at denaturing...
#4 the reagnet is HCl
3. Look at your plot of the data. Which of the four reagents was the most effective at denaturing protein-chromophore complex? Justify your answer. 12 pts] e lon Hc1 was the most effective. This is because it is aston a cid, whrin esuited in the qrcatest ratt of denatoratianc to the othex denaturants. Consider the chemical chain might be chemically changed when the reagent identifned in #3 ts added to the protein. Write properties of...
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...
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....
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form...
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form a triglyceride from glycerol Amino acids combine to form peptides an protonated aater molecule is removed when a carboxylate and and three fatty acids. One and thretis amine react. Figure 1: o- HI Carboxylate reacts with Protonated Amide forming amine 2. Consider the two amino acids, tryptophan and serine bonds can be formed between these acids? How many different peptide 3. Draw each of...
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...
Name: CHEM 131 3. (8 pts) What type of interaction is expected between the side chains of the following pairs of amino acids (examples include salt bridges, H-bonding, disulfide bonds and dispersion forces)? Tyrosine and asparagine a) b) Leucine and proline c) two cysteines Give an example of two amino acids that could form a salt bridge (chemical structure or 3 letter d) code) 4. (10 pts) ldentify in which structural feature (1, 2" or 3" structure) of a protein...
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
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...
#4 the reagnet is HCl
3. Look at your plot of the data. Which of the four reagents was the most effective at denaturing protein-chromophore complex? Justify your answer. 12 pts] e lon Hc1 was the most effective. This is because it is aston a cid, whrin esuited in the qrcatest ratt of denatoratianc to the othex denaturants. Consider the chemical chain might be chemically changed when the reagent identifned in #3 ts added to the protein. Write properties of...
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...
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....
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form a triglyceride from glycerol Amino acids combine to form peptides an protonated aater molecule is removed when a carboxylate and and three fatty acids. One and thretis amine react. Figure 1: o- HI Carboxylate reacts with Protonated Amide forming amine 2. Consider the two amino acids, tryptophan and serine bonds can be formed between these acids? How many different peptide 3. Draw each of...
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...
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