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.
hydrophilic b/c carbohydrates are made of sugars; sugars (such as glucose) have LOTS of hydroxyl groups which are hydrophilic, therefore carbohydrates are hydrophilic
Serine is a conditionally essential amino acid. In other words, humans can synthesize serine under normal nutritional conditions and do not normally need to consume most of the necessary serine in their food. Abbreviated Ser, serine is one of the twenty amino acids that are incorporated into proteins. It is involved in multiple metabolic reactions within the body.
Yes serine is a polar amino acid as it has an hydroxyl group (OH-) attached to the r group.
The terminal hydroxyl group of a steroid is hydrophilic.
It's hydrophilic, due to the hydroxyl functional group in the R group. Though the R group also contains a hydrocarbon group, the hydroxyl group is outermost and thus determines serine's interactions with its environment.
My best guess: Serine. Hydrophilic uncharged pore would let cations and anions pass through.
Mariah Serine is 5' 6".
The serine dehydratase is an enzyme; enzymes act as catalysts in biochemical reactions. Role of serine dehydratase: - transformation of serine in pyruvate - transformation of threonine in propionyl CoA
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.
Carolyn SeRine was born in Salem, in Oregan, USA.
hydrophilic b/c carbohydrates are made of sugars; sugars (such as glucose) have LOTS of hydroxyl groups which are hydrophilic, therefore carbohydrates are hydrophilic
Serine is a conditionally essential amino acid. In other words, humans can synthesize serine under normal nutritional conditions and do not normally need to consume most of the necessary serine in their food. Abbreviated Ser, serine is one of the twenty amino acids that are incorporated into proteins. It is involved in multiple metabolic reactions within the body.
A serine molecule contains information a different number of
It is hydrophilic
Serine does not have any non-bonding electrons pairs. Please click on the related link to see a structural formula for serine.
Hydrophilic