Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching

Article Abstract:

A study presents a systematic examination of tryptophan fluorescence dynamics in proteins with femtosecond resolution, in which distinct patterns of femtosecond-resolved fluorescence transients from the blue to the red side of emission are characterized to distinguish local ultrafast salvation and electronic quenching. Tryptophan is found to be an ideal local optical probe for hydration dynamics and protein-water interactions as well as an excellent local molecular reporter for ultrafast electron transfer in proteins.

Fluorescence, Optical properties, Tryptophan, Structure, Chemical properties

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Ultrafast hydration dynamics in melittin folding and aggregation: Helix formation and tetramer self-assembly

Article Abstract:

The hydration dynamics in different conformations of melittin from a random coil, to a folded alpha-helix, and to self-assembled tetramer is studied using intrinsic tryptophan as a molecular probe. It is observed that the solvation dynamics occurs in 0.62 and 14.7 ps in a random-coiled primary structure, which indicates critical role of hydration dynamics in peptide conformational transitions and protein structural stability and integrity.

Protein folding

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Ultrafast hydration dynamics in the lipidic cubic phase: Discrete water structures in nanochannels

Article Abstract:

Studies of hydration dynamics of confined water in aqueous nanochannels (~50 Angstrom) of the lipidic cubic phase are reported. Results reveal unique water structures and dynamical motions in nanoconfinements, which is critical to the understanding of nanoscopic biological activities and nanomaterial properties.

Water chemistry

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