The transmembrane regions of proteins are predominantly formed by α-helices due to their ability to interact favorably with the hydrophobic core of the lipid bilayer. The α-helix is a stable structure, with hydrophobic side chains extending outward to interact with the lipid bilayer, while the backbone hydrogen bonds stabilize the helix. In contrast, β-sheets are typically seen in specific pore-forming structures like porins and are less common in simple transmembrane domains.
List I | List II |
---|---|
(A) Western Blotting | (II) Protein identification |
(B) Southern Blotting | (I) DNA identification |
(C) Northern Blotting | (IV) RNA identification |
(D) Yeast two-hybrid system | (III) Protein-protein interaction |