Final answer:
The correct conclusion regarding protein shape is that proteins exhibit a variety of shapes due to folding, including helices and beta-sheets, and are influenced by amino acid properties and environmental factors. Not all proteins are helical, and protein folding is crucial for proper function, as misfolding can lead to diseases.
Step-by-step explanation:
Based on the information provided and the protein folding simulation activity, the correct conclusion regarding protein shape is B) Proteins exhibit a variety of shapes due to folding. Proteins do not always fold into a perfect helix; rather, their shape is determined by the sequence of amino acids and their chemical interactions. The alpha-helix is just one type of secondary structure that proteins can form, and it's stabilized by intrachain hydrogen bonding. However, not all proteins have helical structures; some proteins like gamma globulin, chymotrypsin, and cytochrome c have little to no helical structure, while others like hemoglobin and myoglobin are helical in certain regions.
When considering the surface of soluble proteins, one would expect to find amino acids that are hydrophilic, as these will interact favorably with the aqueous environment. Conversely, hydrophobic amino acids tend to be located in the interior of soluble proteins due to their tendency to avoid water. For proteins embedded in a lipid bilayer, such as those within the plasma cell membrane, the exterior surfaces interacting with the lipid tails would be rich in hydrophobic residues, while regions facing the aqueous environment on either side of the bilayer may display hydrophilic residues.
Folding is influenced by environmental factors, and incorrect folding can lead to diseases such as those caused by misfolded proteins. An example of disease resulting from improper protein folding is cystic fibrosis, which is caused by a misfolded CFTR protein, leading to malfunctioning chloride channels and severe respiratory and digestive problems.