Unlike a bar magnet<span>, however, </span>Earth's magnetic field<span> changes over time because it is generated by a geodynamo (in </span>Earth's<span> case, the motion of molten iron alloys in its outer core).</span>
Bacteria! Bacteria! Bacteria! :)
If mutation destroys the function of the Cas9 gene then the bacteria will not be able to target a specific bacteriophage for destruction upon infection for the second time.
<h3>What is the Cas9 gene?</h3>
- Cas9 is a 160 kilodalton protein that plays a vital role in the immunological defense of certain bacteria against DNA viruses and plasmids and is heavily utilized in genetic engineering applications.
- Its main function is to cut DNA and thereby alter a cell's genome.
- Although Cas9 is an endonuclease and is evolved as a mechanism of immunity against viruses, they are not considered restriction enzymes.
To learn more about the Cas9 gene,
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Answer:
Topoisomerase
Explanation:
Topoisomerases are enzymes that produce changes in the topology of the DNA during replication, transcription, traduction, or reparation processes. They can cut one or both strands and in order to relieve torsional stresses in the supercoiled structure of DNA. With this, they help to maintain the chromosome's integrity. There are two types of topoisomerases: topoisomerase I (it cuts only one strand of DNA) and topoisomerase II (it is able to cut both strands of DNA).
Answer:
Hemoglobin rainier differ from normal hemoglobin with respect to oxygen affinity.
Explanation:
Hemoglobin is one of the most significant protein of Red Blood Cell containing heme(that contain Fe2+ which is coordinated with four porphyrine rings) and globin protein.
Hemoglobin exist in two state one is tensed state or deoxy hemoglobin that have less affinity for oxygen, the other state is relaxed state or oxy hemoglobin that has high affinity for oxygen.
In hemoglobin rainer the formation of new di sulfide bond prevent the formation of ion pairs that normally stabilize the T state as a result T state get unstable and this unstable T state is converted to R state to achieve the stability of hemoglobin structure.
The R or relaxed state of hemoglobin has high oxygen affinity for oxygen.
