A new study has revealed the astonishing diversity of protein structures and their folds in nature. The researchers aimed to explore the vast landscape of possible protein topologies and discovered a remarkable array of unexplored protein folds, expanding our understanding of the protein universe.
This research has been published in the journal Nature Structural & Molecular Biology.
Proteins, the building blocks of life, fold into specific three-dimensional structures that enable them to carry out their biological functions. These structures are determined by the amino acid sequences of the proteins. While experimental techniques have successfully uncovered the structures of many proteins, the discovery of new protein folds, characterized by the arrangement and connectivity of α-helices and β-strands, has become increasingly rare. This raises the question: How extensive is the unexplored protein fold space in nature? Theoretical studies have attempted to address this question, but experimental validation is lacking.
To tackle this question, the research team conducted a study that combined theoretical prediction of novel protein folds with experimental validation of their de novo designs.
The research team developed rules based on physical chemistry and protein structure data to theoretically predict possible protein folds. These rules were then used to predict novel αβ-folds, which consist of a four to eight stranded β-sheet and have not yet been observed in the current Protein Data Bank (PDB). This led to the identification of a total of 12,356 novel folds. The team then attempted to computationally design proteins for the predicted novel folds from scratch to assess their foldability and fidelity.
2023-07-13 11:24:02
Post from phys.org