Final answer:
A novel protein with an alpha-helical domain having hydrophobic and hydrophilic faces likely indicates it is a transmembrane protein. The protein's secondary structure, including the alpha-helix, is stabilized by hydrogen bonds which are essential for protein function. The primary structure derived from gene sequences can predict membrane association through hydropathy analysis.
Step-by-step explanation:
The discovery of a novel protein with a single alpha-helical domain featuring hydrophobic amino acids on one side and hydrophilic on the other suggests it could be a membrane-spanning protein. This arrangement is typical for transmembrane proteins, where the hydrophobic face of the alpha helix interacts with the lipid core of the membrane, while the hydrophilic face interacts with the aqueous environment. Notably, the hydrophobic and hydrophilic faces facilitate the protein's integration into and interface with the membrane, respectively.
The secondary structure of proteins such as the alpha-helix and beta-pleated sheet are stabilized by hydrogen bonds. These structures are crucial as they contribute to the overall three-dimensional structure of the protein, which is paramount to its function. Knowing the primary structure of a protein, obtained from the DNA sequence of its gene, allows for a hydropathy analysis which can predict membrane-spanning regions.