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 ...

As a postdoc, Komor found a way to achieve gene-editing with higher efficiencies and a lower incidence of indels by avoiding ...

Researchers led by Université de Montréal pathology and cell-biology professor Marc Therrien have identified major structural ...

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 ...

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

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 ...

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 ...

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 ...

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

That structure is essential for the protein's function. Typically, figuring out the structure involves laborious biochemistry to purify the protein, followed by a number of imaging techniques to ...