Answer:
False.
Explanation:
An Haemoglobin molecule is made up of 4-polypeptides, with each of the polypeptide chain containing an haem group. These haem group can bind with one oxygen atom each.
T<u>he binding of the first oxygen atom by the first haem group weakens the tertiary protein structure of Quaternary structure Hb, thus it makes it easier for the second Oxygen atom to bind faster, and the 3rd oxygen very fast and the 4th oxygen atom the fastest.These accelerated binding of the oxygen atoms, facilitated by the first binding O2, is called cooperative binding.It aids oxygen binding capacity and tranport functions of Hb,</u>
<u />
<u>Myoglobin is an oxygen storage protein in muscles, and not oxygen carrying molecule, It releases stored O2 only in condition of low oxygen supply</u>.It has one haem group in its molecule.Therefore its structural features can not carry out cooperative binding.
Sonya has a chronic illness,
and to treat the condition, she takes an antibiotic every day. Despite her
illness, Sonya’s diet is nutritionally adequate, and she exercises regularly. Based
on this information, Sonya may need to <span>take a
dietary supplement that contains vitamin K.</span>
The structure of the lipid bilayer allows small, uncharged substances such as oxygen and carbon dioxide, and hydrophobic molecules such as lipids, to pass through the cell membrane, down their concentration gradient, by simple diffusion.
Answer:
False
Explanation:
Rearrangements on introns and transposons usually don't cause severe consequences because those sequences are not part of coding genes and therefore cannot code for proteins, and if a rearrangement occur within a coding sequence of a gene might cause an incomplete and non-functional protein causing severe consequences to expression levels of that particular gene.
