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. Fluorescence spectroscopy has been applied to study gelation of different peptides that can be applied as biomaterials.). The questions that we address come from the angle of gelled state (the mixture) vs. solutions of each individual peptide. 1. The local environment of Trp: Is Trp buried in a hydrophobic environment in the gelled state but exposed to the solvent in solution? 2. Does gelation cause anisotropy? 3. Does gelation slow down the rotational motion (flipping) of Trp side chain? 4. Is the Trp is the KA peptide aligned with the Trp in the EA peptide?
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