Proteins exhibit fold-sensitive sets of physical properties
Proteins exhibit fold-sensitive sets of physical properties lead image
Minute changes in the folding patterns of proteins have vast implications for their function and operation. Although folding patterns can be quite varied, there are two commonly occurring folding patterns that are often seen within the protein structure: the curled α-helix and the flat β-sheet. These two folding patterns can be correlated directly to protein function.
Rosenman and Apter detailed how these varied structures lead to a suite of different physical properties and corresponding biological functions. The authors also presented the vast applications.
“We reveal that basic physical properties of proteins are fold-sensitive and demonstrate two completely different sets of physical properties for different folds,” said author Gil Rosenman. “The most surprising thing is that both biological and bioinspired materials demonstrate similar fold-sensitive physical effects.”
Some proteins are not limited to a single fold; instead, they change from one to the other, performing different functions based on their structure. Proteins folded into an α-helix tend to exhibit properties common to dielectric materials, such as piezoelectricity and nonlinear optics.
When these same proteins are refolded into a β-sheet, they instead demonstrate a visible fluorescence effect and optical properties. The fluorescence behavior could help diagnose neurodegenerative diseases such as Parkinson’s and Alzheimer’s diseases, which are caused by certain amyloid proteins which typically have an α-helix misfolded as a β-sheet.
The authors are excited about the potential applications of artificial bioinspired materials in areas like piezoelectricity and integrated photonics. They believe the wide range of properties these materials exhibit will have a large impact on future research.
Source: “Bioinspired materials: Physical properties governed by biological refolding,” by G. Rosenman and B. Apter, Applied Physics Reviews (2022). The article can be accessed at https://doi.org/10.1063/5.0079866 .
