Of the O2 molecules to each one of the four subunits of hemoglobin allosterically regulated. Which of the following is the best explanation for this phenomenon? Affinity of hemoglobin for O2 sensitive to pH. Conformational changes in hemoglobin alter the affinity for O2 the home is positioned in a hydrophobic pocket. Hemoglobin consists mainly of alpha-helices. Change the oxidation state of Fe atoms. What are the Structural levels that are the most different between myoglobin and hemoglobin? Primary and quaternary structure Second and tertiary structure Secondary and tertiary structure Type of prosthetic group and tertiary structure Glycosylation and secondary structure No structural difference where are membranes created in a cell? Phospholipids are added to the outer leaflet of the plasma membrane. Phospholipids are added to the cytoplasmic leaflet of the of the smooth ER membrane. Phospholipids are added to vesicles from lipid droplets. Proteins targeted to the nucleus contain a nuclear localization signal (NLS). What does it do? The NLS is recognized by a translucent at the nuclear membrane that allows the protein to be translocated into the nucleus. The NLS is recognized by soluble \"shuttle\' protein in the cytosol which brings nuclear proteins into the nucleus. The NLS binds the nuclear pore to allow transport into the nucleus. The NLS brings the ribosome .0 dock at the nuclear membrane and the protein is directly synthesized in the nucleus. A triglyceride (three double bonds) A monounsaturated fatty acid An Omega-3 fatty acid A trans fat Cholesterol Solution The iron is in ferous state in haemoglobin. Oxygen temporary and reversibly oxidized ferous into ferric and oxygen temporarily turn into superoxide ion. Ferrioxyhaemoglobin cannot bind oxygen . The enzyme methemoglobin reductase will be able to reducing the iron center. answer... E Myoglobin consists a single polypeptide chain haemoglobin consists several polypeptide chain Myoglobin occurs as monomeric protein haemoglobin occurs as terameric protein. The tertiary structure of myoglobin is similar to a typical water soluble protein structure. Each protein molecule contain one heme prosthetic group and each heme residue contain one central coordinately bound iron atom. answer ...C Cell membrane contain variety of biological molecules including protein and lipid. Fusion of inter cellular vescicals with the membrane incorporate the vesicle membran\'s component into the cell membrane Answer C Nuclear localization signals bind the nuclear pore to allow transport into the nucleus Answer...C The given structure is structure of omega 3fatty acid.

1. Of the O2 molecules to each one of the four subunits of hemoglobin allosterically regulated.
Which of the following is the best explanation for this phenomenon? Affinity of hemoglobin for
O2 sensitive to pH. Conformational changes in hemoglobin alter the affinity for O2 the home is
positioned in a hydrophobic pocket. Hemoglobin consists mainly of alpha-helices. Change the
oxidation state of Fe atoms. What are the Structural levels that are the most different between
myoglobin and hemoglobin? Primary and quaternary structure Second and tertiary structure
Secondary and tertiary structure Type of prosthetic group and tertiary structure Glycosylation
and secondary structure No structural difference where are membranes created in a cell?
Phospholipids are added to the outer leaflet of the plasma membrane. Phospholipids are added to
the cytoplasmic leaflet of the of the smooth ER membrane. Phospholipids are added to vesicles
from lipid droplets. Proteins targeted to the nucleus contain a nuclear localization signal (NLS).
What does it do? The NLS is recognized by a translucent at the nuclear membrane that allows
the protein to be translocated into the nucleus. The NLS is recognized by soluble "shuttle'
protein in the cytosol which brings nuclear proteins into the nucleus. The NLS binds the nuclear
pore to allow transport into the nucleus. The NLS brings the ribosome .0 dock at the nuclear
membrane and the protein is directly synthesized in the nucleus. A triglyceride (three double
bonds) A monounsaturated fatty acid An Omega-3 fatty acid A trans fat Cholesterol
Solution
The iron is in ferous state in haemoglobin. Oxygen temporary and reversibly oxidized ferous into
ferric and oxygen temporarily turn into superoxide ion. Ferrioxyhaemoglobin cannot bind
oxygen . The enzyme methemoglobin reductase will be able to reducing the iron center.
answer... E
Myoglobin consists a single polypeptide chain haemoglobin consists several polypeptide chain
Myoglobin occurs as monomeric protein haemoglobin occurs as terameric protein.
The tertiary structure of myoglobin is similar to a typical water soluble protein structure. Each
protein molecule contain one heme prosthetic group and each heme residue contain one central
coordinately bound iron atom.
answer ...C
Cell membrane contain variety of biological molecules including protein and lipid. Fusion of
inter cellular vescicals with the membrane incorporate the vesicle membran's component into
the cell membrane
Answer C
Nuclear localization signals bind the nuclear pore to allow transport into the nucleus
Answer...C

2. The given structure is structure of omega 3fatty acid