The domain itself adopts an all-α protein fold, a bundle of four alpha helices.

One small area of one protein fold differed from the other.

A helix bundle is a small protein fold composed of several alpha helices that are usually nearly parallel or antiparallel to each other.

The N-terminal domain of TAF has a histone-like protein fold.

Since the globin fold contains only helices, it is classified as an all-alpha protein fold.

H2A utilizes a protein fold known as the 'histone fold.'

Determining the order in which different parts of a protein fold is challenging due to the extremely fast time scales involved.

The morpheein model does not require gross changes in the basic protein fold.

As shown in Figure 1d, the distribution fits the number of distinct functions held by a particular protein fold [ 21, 22].

These prokaryotic proteins, despite having little sequence identity (ThiS has 14% identity to ubiquitin), share the same protein fold.