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1. The primary structure of any protein dictates the overall 3-Dshape of that protein. In class, we discussed secondary, tertiaryand quaternary structure. Please describe in detail how mutationsto the primary structure would alter the higher order structures;provide specific examples of the types of mutations that you madeand what affect it/they would have on the three higher orderstructures. Consider secondary, tertiary and quaternaryindependently (you will have a total of three examples) in youranswer. You may not repeat any mechanism in your three mutantexamples

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Nestor Rutherford
Nestor RutherfordLv2
29 Sep 2019
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Related questions

1) Enzymes are important biological molecules that we have discussed through this course. Describe how the structure of an enzyme can contribute to its specific function within a cell.

a) Dicuss several factors/conditions that could modify the structure and/or function of an enzyme using specific examples (i.e beta-galactosidase/lactase).

b) At the tertiary or quaternary level of organization what would happen if a mutation were to occur in the primary protein sequence coding for an enzyme? Describe different types of mutations that can occur in the protein sequence and how would this affect the different levels of protein folding (structure) and the activity of the enzyme (function)? Remember hemoglobin and what occurs in Sickle cell disease.

Suppose that, in a given protein, one lysine is replaced by aspartic acid. Does this charge occur in the primary structure or in the secondary structure? How might it result in a change in tertiary structure? In quaternary structure? Would this be considered a mutation? In humans mutations can lead to a number of diseases or disorders, please list one and detail/ describe the mutation along with the disease/ disorder.

Some proteins, once folded “associate” to form higher order structures (i.e., quaternary structure). Within these structures the single protein chain is known as a “subunit” (not to be confused with a protein domain). If two identical protein chains fold and associate, the quaternary structure is named “homodimer” (and the individual subunits are sometimes referred to as “monomers”); for three “homotrimer” and so on. If, on the other hand, the two protein chains that associate have different primary structures, the quaternary structure is named “heterodimer”. Using the dimer as an example, we know that the respective regions of the protein subunit surfaces that are interfaced, are responsible for the “favorable energy of interaction” which stabilizes the dimeric protein complex.

(a). Although, noncovalent bonding interactions are used both for stabilization of the folded protein molecule and its dimerization, the contribution of the “hydrophobic effect” to chain folding is significantly greater than its contribution to subunit association. Define the “hydrophobic effect” and explain why you would expect it to have a more pronounced role in chain folding compared to dimerization of the folded molecules.

(b) As the protein chain folds to the native structure, it loses entropy. Upon dimerization, more protein entropy is lost. Compare and contrast the source of protein entropy loss, which occurs with folding, with that which occurs with dimerization.

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