**Core Concept**
An alpha-helix (a-helix) is a type of secondary structure found in proteins, characterized by a spiral conformation stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another. This structure is essential for the stability and function of many proteins.

**Why the Correct Answer is Right**
The correct answer will be the option that does not describe a characteristic of an alpha-helix. In an alpha-helix, the polypeptide backbone is typically **right-handed** (also known as dextrorotatory), with the amino acids arranged in a spiral fashion. The hydrogen bonds between the carbonyl oxygen and amide hydrogen atoms are crucial for maintaining the stability of the alpha-helix structure. Moreover, the alpha-helix is typically **coiled** in a spiral manner.

**Why Each Wrong Option is Incorrect**
* **Option A:** This option may describe a characteristic of an alpha-helix, but without more information, it's hard to say for sure. However, if it describes the structure of an alpha-helix, then it's not the correct answer because we're looking for what's **not true**.
* **Option B:** This option may be a description of a beta-sheet, which is a different type of secondary structure found in proteins. Beta-sheets are characterized by a sheet-like conformation, with the amino acids arranged in a beta-pleated sheet.
* **Option C:** This option may describe a characteristic of a beta-sheet, which is a different type of secondary structure found in proteins. Beta-sheets are characterized by a sheet-like conformation, with the amino acids arranged in a beta-pleated sheet.
* **Option D:** This option may describe a characteristic of a different type of secondary structure or a different aspect of protein structure.

**Clinical Pearl / High-Yield Fact**
It's essential to remember that the secondary structure of proteins, including alpha-helices and beta-sheets, plays a crucial role in their stability, function, and interactions with other molecules.

**Correct Answer:** D.