| STRUCTURE |
Globular proteins, which comprise the majority of known protein structures, appear to share a structural similarity that might help scientists' efforts to verify the accuracy of protein structure simulations. The surfaces of proteins are generally hydrophilic, while their inside cores are hydrophobic. Author finds that the transition from hydrophobic to hydrophilic amino acids occurs at a distance from the protein interior that is spatially proportionate to the protein radius and independent of the size and structure of a number of globular proteins. Because most proteins in human biology are globular, the discovery could be useful in postgenomic proteomics studies. Author notes that his method could also be used to find shared features in proteins with diverse shapes.
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