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 isbroken 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 thatthe 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 bethe 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.

Secondary structure of the proteins: It is the higher level of structural organization of the…

Answered: One technique that is used when…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.
Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.
You're on duty at a prominent Metro laboratory. You mixed up a sample for protein analysis of the samples needed for forensic examination that contains pure DNA while waiting for your closest friend. You decided to use the knowledge you gained in Biochemistry to run the combined samples through a spectrophotometer to eliminate contaminated protein. Determine which of the samples should be extracted and separated for protein analysis based on the following data. Show all of your solutions. A230 A260 A280 Buffer 0.051 0.091 0.065 Sample A 1.27 4.54 2.01 Sample B 1.32 3.92 2.11 Sample C 1.95 3.88 2.04 Sample D 1.44 4.21 2.32
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could giverise to each interaction.(a) Hydrophobic interactions(b) Salt bridges (ionic interactions)
Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
How can the three-dimensional structure of a protein be determined?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?
Protein denaturation usually refers to the disruption of which of the following types of molecular interactions? Select all that apply. A.)Van der Waals attraction B.)Covalent bonds C.)Hydrogen bonds D.)Hydrophobic interactions
Structures of proteins comprising domains separated by flexible linker regions can be quite difficult to solve by x-ray crystallographic methods. Why might this be the case? What are possible experimental approaches to circumvent this barrier?
The primary structure of proteins has polar and non-polar groups. Explain how these groups contribute to developing into the functional 3D protein structure?
What type of information is contained in the three-dimensional structure of proteins? What is the significance of 3D structure prediction? Discuss in depth the key aspects involved in 3D protein structure prediction and computational assessment.
Hydrogen bonding is important at what level of protein structure (primary, secondary, tertiary, or quarternary)? Consider what would happen if there was no hydrogen bonding and just van der Waals in this protein structure. What would you anticipate to happen to its properties? Briefly explain with examples.

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