FLUORINATED AMINO ACIDS IN HELIX-COIL TRANSITIONS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Fluorinated amino acids have applications in both nanotechnology and biotechnology. Their appeal arises from their stabilizing effect on proteins, but the origin of this enhanced stability is not well understood. It has been suggested that the increased hydrophobicity of fluorinated amino acids may account for the increased stability of helical peptides that include them, because the ¿G gained in hydrophobicity is similar to that gained in the overall stability of these peptides. However, the helical propensities of fluorinated amino acids are much lower than their natural counterparts, leading one to believe that the increased stability originates from more that just the hydrophobic effect.