1 a deletion of the first hydrophobic domain would

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encoding the Complex I electron carrier NADH Dehydrogenase. 1. A deletion of the first hydrophobic domain would disrupt the structure of  the signal sequence (an amphiphilic alpha helix) that gets recognized to  import the protein into the mitochondria. Not only would it not be able to  be transported into the mitochondria, but NADH is the first electron donor for the H +  gradient so the ATP synthesis process gets disrupted as well. (C) Deletion of the mitochondrial HSP70 gene. 1. The mitochondrial HSP70 gene is the family of chaperones that aid in the  transport of proteins because they keep proteins unfolded so they may  enter the mitochondria. Transport would not be able to occur without the  HSP70 chaperone, which causes the mitochondrial functions to be  disrupted. (D) Mutation of the N-terminal positively charged amino acids of a subunit of a  mitochondrial ATPase encoded by the nuclear genome. 1. The ampiphilic alpha helix at the N-terminus- with positive- charged  residues on one side and uncharged hydrophobic residues on the other-  gets recognized for entry into the mitochondria. A mutation of the positive amino acids at the N-terminus will disrupt this signal sequence and  transport will not occur.     
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