Structural basis for the enhanced stability of highly fluorinated proteins.

ABSTRACT: Noncanonical amino acids have proved extremely useful for modifying the properties of proteins. Among them, extensively fluorinated (fluorous) amino acids seem particularly effective in increasing protein stability; however, in the absence of structural data, the basis of this stabilizing effect remains poorly understood. To address this problem, we solved X-ray structures for three small proteins with hydrophobic cores that are packed with either fluorocarbon or hydrocarbon side chains and compared their stabilities. Although larger, the fluorinated residues are accommodated within the protein with minimal structural perturbation, because they closely match the shape of the hydrocarbon side chains that they replace. Thus, stability increases seem to be better explained by increases in bur

SUBMITTER: Buer BC 

PROVIDER: S-EPMC3324029 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature