Which type of secondary structure would the polypeptide sequence below most likely form? VCITWHFRAQGTFELSVE please explain
Which type of secondary structure would the polypeptide sequence below most likely form? VCITWHFRAQGTFELSVE
please explain
Homework Answers
The most common types of secondary structures are the α helix and the β pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another.
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Which type of secondary structure would the polypeptide sequence
below most likely form? VCITWHFRAQGTFELSVE
please explain
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...
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...
Briefly explain the difference between primary, secondary, tertiary and quaternary polypeptide structure is.
Briefly explain the difference between primary, secondary, tertiary and quaternary polypeptide structure is.
Question 13 (1 point) Given the following sequence, what secondary structure does it most likely prefer,...
Question 13 (1 point) Given the following sequence, what secondary structure does it most likely prefer, and where in a protein would it most likely be found? WFIVMWFILFAY 1) B-strand on the surface of the protein 2) B-strand in the interior of the protein O 3) a-helix in the interior of the protein 4) a-helix on the surface of the protein Question 14 (1 point) Enzymes are potent catalysts because they: 1) lower the activation energy for the reactions they...
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10)...
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10) (15) (20) lys Lys Ala-Phe-Trp-Met-His- GIh-Thr-lle-Arg-Ser-Gly-Ala-Gly-Ser-Gly-Ala-Trp-Tyr-Pro-Val-Ala (30) Phe-Met-Leu-Val-Pro-Glu-Glu There are at least two regions where alpha helical structure is found. Indicate the beginning and ending residues of these regions. Any group or groups which break the alpha helical structure should not be considered part of the helix. Remember that it take four residues to give a turn of an alpha helix, so that is...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form a folded structure stabilized primarily by a disulfide linkage. a. Draw the folded structure (using circles) and illustrate the disulfide bond. Asp Met LeuCys Gly GlyY Val IleTyrXSerVal CysPhe b. What level of protein structure is being illustrated in the folded forrm? Primary, secondary, tertiary, or quaternary? c. What other type of intramolecular interaction might stabilize the folded form of this polypeptide? 4. The...
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...
which of the following is not a way in which amino acid structure in sequence might...
which of the following is not a way in which amino acid structure in sequence might affect the properties of a protein a) Amino acid side chains form peptide bonds with each other causing the molecule to twist into a secondary structure b) Amino side chains interact with each other causing polypeptides to bend into a tertiary structure c) Hydrogen bonding between every fourth amino acid results in the formation of a coil called an a helix d) Hydrogen bonding...
What is most likely to differ between two different genes? Select all correct answers. The primary...
What is most likely to differ between two different genes? Select all correct answers. The primary sequence of the polypeptide they provide information to generate The sequence of nucleotides in the section of DNA The location on the chromosome The type of protein they provide information to generate The folding and overall structure of the polypeptide they provide information to generate The overall length - such as 100 bases versus 8,000 bases The type of monomers found within the section...
The answer is C but why? 15. Below is the middle region of a particular polypeptide....
The answer is C but why?
15. Below is the middle region of a particular polypeptide. The wild-type amino acid sequence and the sequence of several mutant polypeptides are given ( ... indicates additional, unspecified amino acids). Which of the five mutant polypeptides is most likely to be the result of a nonsense mutation in the corresponding gene? a. mutant 1 b. mutant 2c. mutant 3d. mutant 4e. mutant 5
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...
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...
Question 13 (1 point) Given the following sequence, what secondary structure does it most likely prefer, and where in a protein would it most likely be found? WFIVMWFILFAY 1) B-strand on the surface of the protein 2) B-strand in the interior of the protein O 3) a-helix in the interior of the protein 4) a-helix on the surface of the protein Question 14 (1 point) Enzymes are potent catalysts because they: 1) lower the activation energy for the reactions they...
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10) (15) (20) lys Lys Ala-Phe-Trp-Met-His- GIh-Thr-lle-Arg-Ser-Gly-Ala-Gly-Ser-Gly-Ala-Trp-Tyr-Pro-Val-Ala (30) Phe-Met-Leu-Val-Pro-Glu-Glu There are at least two regions where alpha helical structure is found. Indicate the beginning and ending residues of these regions. Any group or groups which break the alpha helical structure should not be considered part of the helix. Remember that it take four residues to give a turn of an alpha helix, so that is...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form a folded structure stabilized primarily by a disulfide linkage. a. Draw the folded structure (using circles) and illustrate the disulfide bond. Asp Met LeuCys Gly GlyY Val IleTyrXSerVal CysPhe b. What level of protein structure is being illustrated in the folded forrm? Primary, secondary, tertiary, or quaternary? c. What other type of intramolecular interaction might stabilize the folded form of this polypeptide? 4. The...
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...
The answer is C but why?
15. Below is the middle region of a particular polypeptide. The wild-type amino acid sequence and the sequence of several mutant polypeptides are given ( ... indicates additional, unspecified amino acids). Which of the five mutant polypeptides is most likely to be the result of a nonsense mutation in the corresponding gene? a. mutant 1 b. mutant 2c. mutant 3d. mutant 4e. mutant 5
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