A protein has a precisely defined amino acid sequence which gives rise to its three dimensional structure which is essential to the protein’s function. These amino acids interact with one another to produce a specific folding pattern that produces the conformation of the protein. When one looks at the progression a protein makes in its folding complexity, it is clear that the folding is driven by the amino acid sequence alone.
To understand this concept it is best to start with the primary structure of the protein, the polypeptide chain. The first interaction the amino acids make, a peptide bound, is the first instance where protein folding is directed. Two amino acids are joined together through a condensation reaction producing a peptide …show more content…
These interactions can include weak interactions such as hydrogen bonds, ionic bonds and van der Waals forces, and also covalent bonds between two cysteine amino acids called a disulfide bond (Tymoczo et al., 2013). Similar the secondary structure, the interactions available are completely determined by the types and order of amino acids in the peptide chain; however, in the tertiary structure the interactions are between the R groups of the amino acids not the main chain. The amino acid sequence’s interaction with the environment also contributes to the tertiary structure of the protein. For instance, if the protein is in an aqueous solution it will fold in such a way to bring its nonpolar amino acids into the interior and arrange the polar amino acids on the exterior; this is referred to as the hydrophobic effect (Tymoczo et al., 2013). The environment can also contribute to the way amino acids arrange themselves in the overall tertiary structure of the protein. Even though the protein is becoming more intricate, the folding is still driven by the basic building blocks of the protein. If a protein only consists of one polypeptide chain, then the tertiary structure is the highest degree of complexity the protein can achieve; however, if there is more than one polypeptide a quaternary structure …show more content…
Replacing an amino acid on any part of the sequence can have detrimental affects on the conformation and function of the protein. Sickle cell anemia, which results from just a single amino acid change, from a glutamic acid to a valine, causes the red blood cells in an affected individual to fold improperly and form a sickle cell shape. This shape causes the cells to die early and aggregate and clog blood vessels resulting in decreased oxygen flow in the affected individual. This leads to pain and other serious problems such as infection, acute chest syndrome and stroke (CDC, 2014). Even a change as small as one amino acid can affect entire physiological functions. One can also disrupt the function of a protein by changing its physical environment, such as heating or altering the pH, or through chemical disruptions using urea or β-mercaptoethanol, all of which will disrupt the interactions of the amino acids and lead to an overall loss of function in the
To understand this concept it is best to start with the primary structure of the protein, the polypeptide chain. The first interaction the amino acids make, a peptide bound, is the first instance where protein folding is directed. Two amino acids are joined together through a condensation reaction producing a peptide …show more content…
These interactions can include weak interactions such as hydrogen bonds, ionic bonds and van der Waals forces, and also covalent bonds between two cysteine amino acids called a disulfide bond (Tymoczo et al., 2013). Similar the secondary structure, the interactions available are completely determined by the types and order of amino acids in the peptide chain; however, in the tertiary structure the interactions are between the R groups of the amino acids not the main chain. The amino acid sequence’s interaction with the environment also contributes to the tertiary structure of the protein. For instance, if the protein is in an aqueous solution it will fold in such a way to bring its nonpolar amino acids into the interior and arrange the polar amino acids on the exterior; this is referred to as the hydrophobic effect (Tymoczo et al., 2013). The environment can also contribute to the way amino acids arrange themselves in the overall tertiary structure of the protein. Even though the protein is becoming more intricate, the folding is still driven by the basic building blocks of the protein. If a protein only consists of one polypeptide chain, then the tertiary structure is the highest degree of complexity the protein can achieve; however, if there is more than one polypeptide a quaternary structure …show more content…
Replacing an amino acid on any part of the sequence can have detrimental affects on the conformation and function of the protein. Sickle cell anemia, which results from just a single amino acid change, from a glutamic acid to a valine, causes the red blood cells in an affected individual to fold improperly and form a sickle cell shape. This shape causes the cells to die early and aggregate and clog blood vessels resulting in decreased oxygen flow in the affected individual. This leads to pain and other serious problems such as infection, acute chest syndrome and stroke (CDC, 2014). Even a change as small as one amino acid can affect entire physiological functions. One can also disrupt the function of a protein by changing its physical environment, such as heating or altering the pH, or through chemical disruptions using urea or β-mercaptoethanol, all of which will disrupt the interactions of the amino acids and lead to an overall loss of function in the