Chemistry A homotetramer (lacking intermolecular covalent interactions) has a native molecular size of 60 kDa. What is the expected molecular size of this protein when analyzed by SDS-PAGE? a) 30 kDa b) 240 kDa c) 60 kDa d) 15 kDa
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Chemistry
A homotetramer (lacking intermolecular covalent interactions) has a native molecular size of 60 kDa. What is the expected molecular size of this protein when analyzed by SDS-PAGE?
a) 30 kDa
b) 240 kDa
c) 60 kDa
d) 15 kDa
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- Intramolecular ______ are responsible for formation of the most common three-dimensional shape in proteins, the alpha helix. a) van der waals forces b) hydrogen bonds c) covalent bonds d) ionic (electrostatic) interactionsChemistry Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be substituted by N without affecting the conformation? b) Which residue(s) can be substituted by D without affecting the conformation? c) Which residue(s) cannot be substituted without affecting the conformation?According to scientist, the first three protein structures resemble a TELEPHONE CORD, try to envision the protein structure (primary, secondary, tertiary) and discuss using your own words the analogy on why do you think the structure resembles the cord of a telephone.
- Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryDescribe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?At what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)
- If you heat a protein to break the intramolecular hydrogen bonds, will you maintain the a-helical or b-sheet structure?Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?Most proteins denature at high temperatures. A. Are peptide bonds typically broken at high temperatures, yes or no? _________________ B. Does denaturation disrupt the primary structure of a protein, yes or no? __________________ C. Why do proteins denature at high temperatures? D. Is it likely that a denatured protein is able to perform its physiological function, yes or no? Why or why not? Thoughtfully defend your answer.
- Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryoelectron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?Protein Structure Describe the four levels of protein structure: Primary, secondary, tertiary, and quarternary.You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.
