Transmembrane Protein Lab Report

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Extra credit 1). Propose an experiment to test the importance of this property for transmembrane protein insertion and orientation. Up to 2.5 pts¬¬ Generally, transmembrane proteins tend to be solubilized only by agents that disrupt hydrophobic associations and destroy the lipid bilayer. The most efficient substance to use are detergents, because they are small amphipathic molecules that tend to form micelles in water. This experiment will be intended to define the unfolded state of a transmembrane protein and see if they adopt different types of amphiphilic structures. I will create an experiment to determine if the unfolded state of membrane proteins in detergent micelles is different from that in the thermal denaturation experiments. When …show more content…

Propose a simple experiment to demonstrate that the location of the positive (basic) amino acids determines the orientation of the transmembrane segment as shown above. Up to 2.5 pts An experiment that would demonstrate that the location of the positive (basic) amino acids determines the orientation of the transmembrane segment would be to have multiple polypeptide protein chains that are very similar in their amino acid sequence. All the amino acids in the protein chain would share similarity except for the amino acid that flanks the start transfer sequence. By altering the flanking amino acid on the STS with an amino acid that has a differing polar property and charge, it will alter the way the protein inserts into the membrane as well how it folds itself. By having positively charged amino acids before the STS is attached or after its attached, you will different orientations of polypeptide chain segments embedded into the

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