Oxygenation said she would not like to me because I
Explanation:
Carbon dioxide is added to the atmosphere naturally when organisms respire or decompose (decay), carbonate rocks are weathered, forest fires occur, and volcanoes erupt. Carbon dioxide is also added to the atmosphere through human activities, such as the burning of fossil fuels and forests and the production of cement.
Answer:
Molecular Evidence has recently made it necessary to assign the prokaryotes to either of two different domains.
Explanation:
- There was an OLD 5 classification system :
- Monera
- Protists
- Plants
- Fungi
2. NEW 3 domain system reflects :
- A greater understanding of evolution
- Molecular evidence
Thus, the new domain includes :
- Prokaryote : Bacteria
- Prokaryote : Achaebacteria
3. Eukaryotes :
- Protists
- Plants
- Fungi
- Animals
Answer:OWA OWA
Explanation:Thanks lol and if anyone can help me on my recent questions please thanks<3
Out of the following given choices;
In allosteric inhibition, a regulatory molecule binds to a
location other than the active site, resulting in a change in enzyme shape that
allows the active site to bind substrate.
In allosteric activation, a regulatory molecule binds to a
location other than the active site, resulting in a change in enzyme shape that
allows the active site to bind substrate.
In allosteric inhibition, a regulatory molecule binds to the
active site, blocking substrate binding.
In allosteric activation, a regulatory molecule binds to the
active site, allowing substrate binding.
The answer is B. When an effector molecule binds to an
allosteric site, the enzyme changes conformation
causing the enzyme to have a high affinity
for its ligand at the active site. A good
example to explain allosteric regulation is hemoglobin
(which is not an enzyme though). The
subunits of the hemoglobin have
allosteric effects on each other. When oxygen
binds to one subunit, its conformation change
causing the subunit to bind to the allosteric
site of adjacent subunits. This subsequently causes the other subunits to have
more affinity for oxygen in their oxygen-binding
active sites.
