Alanine is very hydrophobic as it is non-polar at its (medium sized) side chain. This means it will most often be found in the internal regions of a globular protein in an aqueous solution, as it will become buried during the hydrophobic collapse of the early stages of protein folding. There will be exceptions to this when the majority of amino acids near it in the polypeptide chain are hydrophilic.
Serine has a polar hydroxyl group, making it slightly hydrophilic. You would therefore expect it to appear on the surface of the protein more often, or lining aqueous channels. It is only a little hydrophilic though, so it would not be surprising to find a more even distribution of serine around both the internal regions and external surfaces of the protein. More importantly though, the hydroxyl group of serine can be very reactive, particularly in certain environments produced by surrounding amino acids. Since it is very reactive, it is a common components of the catalytic (active) site of enzymes. For example, the catalytic triad of some protease enzymes.
haemoglobin is considered as globular protein because it has ametabolic functions and considered as conjugated protein because it cosisted of protein and non protein moiety
fibrous
globular proteins .
Actin is a globular molecule
Globular
A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by Hydrogen Bonds.
Serine, being hydrophilic, will be more likely to appear near the surface of a globular protein in solution, and alanine, being hydrophobic, will more likely appear near the centre of the protein. This illustrates the "hydrophobic effect", which is one of the effects that stabilizes the tertiary and quaternary structures of proteins. The hydrophobic effect is not due to an intramolecular force but the tendency of hydrophilic and hydrophobic amino acids to interact oppositely with water and segregate into surface and inner regions.
glubour
haemoglobin is considered as globular protein because it has ametabolic functions and considered as conjugated protein because it cosisted of protein and non protein moiety
Tritiory proteins are globular proteins. Every enzyme is a globular proteins.
fibrous
the low concentration of salt increases the protein solubility on aqueous solution,known as salting in effect
No
globular proteins .
Actin is a globular molecule
No, collagen is a Fibrous protein. An example would be insulin.
alanine, arginine, cystine, leutine, etc...