An intrinsically disordered protein (IDP) is a protein that lacks a fixed three- dimensional structure. Estimate the size of an IDP of 100 amino acids by calculating the most probable end-to-end length of the protein. Assume the protein is a freely-joined chain with the length of each segment (amino acid) b = 3Å.
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- Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientationsMatch the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondaryAssume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. ΫΠΙ ΑΣΦ ха хь a b 1.73 106 ● Ĵ √x x X X |X| wwwww Submit Previous Answers Request Answer ? X.10n X orientations The problem is essentially asking about the possible combinations given that you are selecting one of three items a set number of times. It may help to think of a concrete example. If you roll a standard six-sided die, the first roll has six possible combinations. The second roll also has six possible combinations; however, when paired with the first there are 6 x 6 possible sets of numbers. Provided the order of the numbers matters, when rolling a third time there are 6 x 6 × 6 possible sets of numbers. This pattern is 6" where r is the number of rolls. For this problem, there are three possible selections. There are 120…
- 3a) The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This will incorporate any 2° structure the protein has, but is predominantly the result of side-group interactions. Name the type of interaction, if any, that you would expect to see under physiological conditions (an aqueous solution at pH 7.0-7.5) between the following pairs of amino acid side groups. Serine and asparagine: Methionine and lysine: Glutamate and aspartic acid: Alanine and phenylalanine:Describe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.One technique that is used when attempting to solve the crystal structure of a large protein is not to solve the structure of the whole protein itself. Instead, the protein is broken down into smaller components and the structure of the smaller components is what is solved. Of course, when performing this technique, it must be ensured that the process of breaking down the protein into smaller components does not drastically change the structure of the smaller components. With this in mind, where would be the best locations to cut a protein? At the beginning and end of secondary structures. At beginning and end of protein domains. O At the beginning and end of motifs. At the beginning and end of protein subunits.
- 3a) Secondary (2°) structure in proteins refers to two specific conformations a region of a protein can take on, the a-helix and the b-pleated sheet. Briefly describe or explain how 2° structure forms/what causes 2° structure to form in a region of a protein.A protein with a known mass of 240 kDa is treated with -mercaptoethanol, a sulfhydryl reducing agent. When the resultant peptide mixture was analyzed by SDS PAGE, one protein band of 60 kDa was present. How many disulfide bonds were present in the original structure of the protein? Group of answer choices -4 -2 -1 -3TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
- Researchers investigating the protein composition in mice have identified a new protein and found evidence of sulfur-containing cysteine at regular intervals in its primary structure. Which of the following best describes the most direct significance of this finding? A B с D The secondary structure of the protein will include tightly would alpha-helices but no beta sheets. The tertiary structure of the protein likely contains a relatively high number of bends and angles. The protein will form a relatively highly stable tertiary structure. The dietary intake of mice must include the regular ingestion of cysteine.Among the many different biological functions of proteins, identify and describe two (2) general functions. Explain how theprotein structure relates to these functions. Cite a particular protein that exhibits each function you have described and give the unique features of its primary, secondary, tertiary, and quaternary (if applicable) structures.A protein with a known mass of 240 kDa is treated with beta-mercaptoethanol, a sulfhydryl reducing agent. When the resultant peptide mixture was analyzed by SDS PAGE, one protein band of 60 kDa was present. How many disulfide bonds were present in the original structure of the protein? Group of answer choices 4 2 1 3