I'm desperate and I cannot find the answer to this question....
As the name implies, globular proteiens tend to have a roundish, globular shape. What types of side chains might you expect to find on the amino acid residues that face the outside of a globular protein if it is primarily found in an aqueous environment in the body? What type of side chains might be found facing the inside?
Please HELP ASAP!!
I'm desperate and I cannot find the answer to this question....
As the name implies, globular proteiens tend to have a roundish, globular shape. What types of side chains might you expect to find on the amino acid residues that face the outside of a globular protein if it is primarily found in an aqueous environment in the body? What type of side chains might be found facing the inside?
Please HELP ASAP!!
To understand the types of side chains you might expect to find on the amino acid residues that face the outside and inside of a globular protein, we need to consider the principles of protein folding and the interactions involved in stabilizing the protein structure.
When a globular protein is in an aqueous environment, the amino acid residues on the outside of the protein are likely to be exposed to water molecules. To effectively interact with water, these residues usually have hydrophilic or polar side chains. Hydrophilic side chains have a strong affinity for water molecules and can form hydrogen bonds with them. Examples of amino acids with hydrophilic side chains are serine (Ser), threonine (Thr), asparagine (Asn), glutamine (Gln), and lysine (Lys). These side chains contain polar groups and can form hydrogen bond interactions with water molecules.
On the other hand, the amino acid residues that face the inside of the protein tend to be shielded from the solvent and are generally buried within the protein's core. These residues are not in direct contact with water and are typically hydrophobic in nature. Hydrophobic side chains repel water and prefer to interact with other hydrophobic residues. Amino acids such as alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), phenylalanine (Phe), and tryptophan (Trp) have hydrophobic side chains.
It's important to note that this is a general trend, and some exceptions may exist depending on the specific protein and its function.
To find additional information or verify the details for a particular protein, you can consult scientific literature, books on protein structure and function, or online databases such as the Protein Data Bank (PDB) which provides information on the three-dimensional structures of proteins.