Answer:
- Interactions of the hydrophobic and hydrophilic amino acids help to anchor the protein in the membrane.
Explanation:
The above statement correctly defines that it is significant to fold protein correctly in the transmembrane protein as displayed above because the 'interactivity along the hydrophilic and the hydrophobic amino acids assist in harboring the protein in the membrane.' These 3-dimensional structures have a specific biological significance and promote better functioning. The incorrect folding of protein may give rise to numerous diseases.
Interactions of the hydrophobic and hydrophilic amino acids help to anchor
the protein in the membrane is the statement that best explains why correct
protein folding is critical in the transmembrane protein.
Protein consists of amino acids in a 3 dimension form and its correct folding
aids its optimal functioning. In a protein structure, there are interactions of
the hydrophobic and hydrophilic amino acids which acts as a strong anchor.
The hydrophobic parts of amino acids help to interact with the long chains
of the fatty acids in lipid bilayer while the hydrophilic part of amino acids
assist to interact with water on the surface of the cell membrane.
Read more on https://brainly.com/question/25076473
