iew this skill exercise as an o n. Therefore the justification will important as
ID: 149458 • Letter: I
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iew this skill exercise as an o n. Therefore the justification will important aspect of your answer tor may assign one or more of these questions: our instructor contributes to the favorable free energy change that makes protein folding a eous in a nonpolar solvent, would it have the same structure as the same protein 3 Ifa protein were placed nonpolar solvent placed in water? Justify your answer and contrast the entropy changes of the dissolution of the followin Compare phenylalanine and aspartate (in water). g two amino acids s. The graph below shows nergy information with thermodynamic parameters involved in a macromolecular interaction. Propose a type of interaction that matches these data with thermodynamic 60 40 S 20 -20 -40Explanation / Answer
1) Water has high dielectric constant because of which the hydrogen bonding will inrease between the amino acids and water. It also increases the hydrophobic forces between the hydrophobic residues which is the driving force for protein folding. Together hydrogen bonding, hydrophobic force and vanderwaal force help in making the process spontaneous and thus drive the protein folding. During protein folding hydrophobic amino acids will move to the protein core to minimize the contact with water and hydrophillic amino acids will intract with water.
2) if a protein is placed in non polar solvent all hydrophobic amino acids will be present on the outer surface and hydrophilic amino acids will be in the core. This process is non as phase inversion. And the structure of the protein will be different to that of the water soluble protein.
3) In water aspartic acid will make interactions will water and hence the entropy of aspartate will decrease. The dissolution of phenylalnine can be possible only by providing energy. It is a highly entropic effect. Dissolution of both amino acids will make free water species less available.
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