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 ...

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 ...

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 ...

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 ...

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

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

An artificial protein moves between predetermined conformations when exposed to calcium ions. These dynamic structural ...

“Alpha helix proteins are especially important. Their spring-like structure gives them elasticity and resilience, which is why skin, hair, feathers, hooves, and even cell membranes are so durable.

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 ...