Figure 1: Hyperactivity of insect antifreeze protein compared to a fish antifreeze protein. Figure 3: Ice hemispheres and an ice crystal grown in the presence of slow AFP. Figure 4: SbwAFP model ...

Most proteins are left-handed, but scientists have found an ancient molecule that works in both mirror-image forms.

In a new move, researchers have shown that protein design software can incorporate motion into its outputs. The resulting ...

which can affect the folding and three-dimensional shape of the protein. There are two main things that can alter the secondary structure: α-helix: N-H groups in the backbone form a hydrogen bond ...

A protein’s amino acid sequence helps determine its structure. Thus ... can cause a protein fold to switch from an α-helix to a β-sheet or vice versa. Lauren L. Porter of the National ...

An unusual protein structure known as a 'rippled beta sheet ... Certain common structural motifs, such as the alpha helix, are found in many protein structures. The rippled sheet is a variation ...

The most common secondary protein structure is the α-helix, which can coil to the right (P) or left (M). This coiling direction in turn determines how it engages with other chiral structures ...

AlphaFold (Panel B) takes as input the 1D sequence of a protein of unknown structure and a multiple sequence alignment (MSA) of many similar proteins found in different species and tissues.