Answer:
A few obstacles would make it tough to accomplish this objective. In the first place, the polypeptide backbone is characteristically polar. Hardly any proteins would be dissolvable in a non-polar hydrocarbon. Moreover, to keep up the dissolvability of this protein, most of its amino acids would need to contain hydrophobic or non-polar R groups.
Then again, its charged or polar R groups would need to connect with one another or be covered in the core of the protein away from the hydrocarbon solvent. This would put noteworthy requirements on both the idea of the R groups and the structure of the protein that could take part in substrate recognition or catalysis. By and large, this is certainly not a reasonable objective.
Answer:
Instead of oxygen a creature would also need nutrients. Simple everyday things like water and food.
Explanation:
Although it is kind of impossible to live without oxygen. There are organisms on the earth who do not need it and can survive. They metabolize hydrogen or methane or a number of other compounds.
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.
