Matrix Effects on Spin−Lattice Relaxation in the Triplet State of Tryptophan
Author:
Affiliation:
1. Department of Chemistry, University of California, Davis, California 95616
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp971455m
Reference19 articles.
1. Phosphorescence and optically detected magnetic resonance studies of a class of anomalous tryptophan residues in globular proteins
2. Techniques, Theory, and Biological Applications of Optically Detected Magnetic Resonance (ODMR)
3. [25] Optically detected magnetic resonance of photoexcited triplet states
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1. Spin−Lattice Relaxation of the Tryptophan Triplet State Varies with Its Protein Environment;The Journal of Physical Chemistry B;2002-04-18
2. Characterization of the Tryptophan Residues of Escherechia coli Alkaline Phosphatase by Phosphorescence and Optically Detected Magnetic Resonance Spectroscopy;Biochemistry;2001-11-10
3. Dynamic nuclear polarization by photoexcited-triplet electron spins in polycrystalline samples;Chemical Physics Letters;2001-09
4. Band-Shape Analysis of Delayed Slow-Passage ODMR in the Photoexcited Triplet State of Tryptophan;The Journal of Physical Chemistry B;2000-01-14
5. Ligand-Induced Conformational Changes in Lactose Repressor: A Phosphorescence and ODMR Study of Single-Tryptophan Mutants;Biochemistry;1999-04-29
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