I think the correct answer from the choices listed above is the first option. THe tool that would be <span>useful for testing cleavage and fracture in a mineral would be a hammer. It can test how a mineral acts when subjected to a very large amount of pressure or force. Hope this answers the question.</span>
One option is that the samples run through gel electrophoresis is too small to be recognized (shorter strands of DNA travel further through the gel and larger strands travel shorter). The other option in that the restriction enzyme did not cut the DNA in the proper spot or there was a mutation in the bases that allowed for a mistake in the cutting; that is why there are 800 base pairs in one sample (that's a lot) An example of a mutation is that lets say the restriction enzyme was supposed to cut at the second G in GGACC. But if that G was turned into an A, then the restriction enzyme wouldn't cut there.
For number 5, you might have 800 because of the restriction enzyme cutting it wrong, a mutation that allowed for the cutting to not take place, or a fault in the sample taking.
I am an AP Biology student right now in Wisconsin. I just finished that worksheet this morning :) anymore questions just hit me up
D. The input of solar energy can be added
Answer:
The correct answer is "proteins in which isoleucine is inserted at some positions normally occupied by leucine".
Explanation:
The missing options of this question are:
A. proteins in which leucine is inserted at some positions normally occupied by isoleucine.
B. proteins in which isoleucine is inserted at some positions normally occupied by leucine.
C. no abnormal proteins, because the ribosomal translation machinery will recognize the inappropriately activated tRNAs and exclude them from the translation process.
D. no proteins, because the inappropriately activated tRNAs will block translation
The correct answer is option B. "proteins in which isoleucine is inserted at some positions normally occupied by leucine".
In normal conditions, the enzyme leucyl-tRNA synthetase attaches one leucine amino acid to leucyl-tRNA as part of synthesis of proteins that have one or more leucine residues in their sequences. Since the enzyme of this mutant strain of bacteria mistakenly attaches isoleucine to leucyl-tRNA 10% of the time, approximately 10% of all the proteins that normally have leucine residues will going to have isoleucine. Therefore, These bacteria will synthesize proteins in which isoleucine is inserted at some positions normally occupied by leucine.
They are created by the physical/chemical alteration by heat and pressure of an existing igneous or sedimentary material into a more denser form. (In other words, they are igneous or sedimentary rocks that have undergone changes as a result of extreme pressure and heat.)
