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Optica Publishing Group
  • Quantum Electronics and Laser Science Conference
  • OSA Technical Digest (Optica Publishing Group, 1989),
  • paper TUGG31

Long-range nonradiative energy transfer from tryptophan triplet states for protein structure studies

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Abstract

The use of nonradiative diffusion enhanced energy transfer (DEET)1 has been demonstrated to be a useful tool for the study of the protein structure. However, the time scale for DEET is determined by spatial diffusion of acceptor molecules in the vicinity of the donor molecules and is typically of the order of milliseconds. Hence, if quenching of optical emission lifetimes of the donor molecule is used to determine distances between acceptor and donor molecules, the intrinsic emission lifetime of the donor molecule must be longer than the characteristic time for DEET. Previous work has been based on the use of long-lived states of donor molecules or atoms bound to the protein or transfer of the energy of donor molecules or atoms in the solution to acceptor molecules bound to the protein.

© 1989 Optical Society of America

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