0
Why are residues hydrophobic in myoglobin but hydrophobic in hemoglobin?
Wiki User
∙ 8y agoWant this question answered?
Be notified when an answer is posted
Add your answer:
Earn +20 pts
What protein inside red blood cells binds oxygen?
Hemoglobin
How many oxygen molecules bind to myoglobin?
1 Each myoglobin molecule has one heme group and can bind one oxygen molecule. Hemoglobin on the other hand can bind up to 4 molecules of oxygen.
What is oil drop model of a protein?
The oil drop model for proteins basically refers to the fact that in water, oil sticks together to form an oil droplet rather than being dispersed throughout the water in many droplets. Why? - Because of the hydrophobic effect. hydrophobic hydrocarbon chains cause water to form "cages" around them (this is because water cannot hydrogen bond to the protein so makes extra hydrogen bonds to itself), becoming more ordered and therefore losing entropy (S) which is unfavourable. This is the same for hydrophobic residues in the protein chain. If exposed, water will become ordered around them, losing entropy. The hydrophobic effect aims to minimise this entropic loss by burying the hydrophobic residues within the core of the protein. Hydrophobic residues can form relatively strong Van der waals forces with each other while the polar residues can form H-bonds with the water molecules.
What is the biological term of oxygen carrying pigment found in red blood corpuscles?
heomoglobin..... a comlex compound of proteins with iron......
What is irons main function in the body?
hemoglobin and myoglobin are 2 types of iron in the human body.
One advantage hemoglobin has over myoglobin as a respiratory pigment is that?
Cooperative binding. Hemoglobin can load and unload oxygen better than myoglobin. So it is kore sensitive to changes in the environment, vs. Myoglobin
What is the iron containing protein that is found in red blood cells and carries oxygen from the lungs?
The iron-containing protein found in red blood cells that carries oxygen is called hemoglobin.
What protein inside red blood cells binds oxygen?
Hemoglobin
What is the percent similarity of myoglobin and hemoglobin How much are they alike?
54
What red protein is related to hemoglobin that supplies O2 molecules?
Myoglobin
A mineral that is a component of hemoglobin myoglobin and cytochromes is?
iron. thanks for this quick answer.
What does myoglobin do for muscles?
Myoglobin's function is similar to that of hemoglobin, which carries oxygen in red blood cells to various tissues. Myoglobin has even higher affinity for oxygen than hemoglobin and is specific to muscle cells. Myoglobin thus acts as a storage of oxygen, as it holds oxygen inside heart and skeletal muscles.
What compound stored oxygen inside skeletal muscle cells?
keratinThe correct answer is NOT keratin... the correct answer is myoglobin. This is the oxygen-binding pigment in muscle.
Difference of myoglobin and hemoglobin?
myoglobin: the molecule is compact there is no water inside it with the exception of a very small number(less than 5) of single water molecules presumably trapped at the time the molecules is folded up. hemoglobin: it iz 4 times larger than myoglobin. it is spherical molecule formed by 4 subunits which are identical in pairs . each subunits has a conformation closely resembling that of myoglobin and the aggregation is held together by extensive van der waals forces.
How many oxygen molecules bind to myoglobin?
1 Each myoglobin molecule has one heme group and can bind one oxygen molecule. Hemoglobin on the other hand can bind up to 4 molecules of oxygen.
What is oil drop model of a protein?
The oil drop model for proteins basically refers to the fact that in water, oil sticks together to form an oil droplet rather than being dispersed throughout the water in many droplets. Why? - Because of the hydrophobic effect. hydrophobic hydrocarbon chains cause water to form "cages" around them (this is because water cannot hydrogen bond to the protein so makes extra hydrogen bonds to itself), becoming more ordered and therefore losing entropy (S) which is unfavourable. This is the same for hydrophobic residues in the protein chain. If exposed, water will become ordered around them, losing entropy. The hydrophobic effect aims to minimise this entropic loss by burying the hydrophobic residues within the core of the protein. Hydrophobic residues can form relatively strong Van der waals forces with each other while the polar residues can form H-bonds with the water molecules.
What is the biological term of oxygen carrying pigment found in red blood corpuscles?
heomoglobin..... a comlex compound of proteins with iron......
