1976
DOI: 10.1038/261521a0
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Kinetics of triplet–triplet energy transfer and intramolecular distances in enzyme–inhibitor complexes

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Cited by 14 publications
(3 citation statements)
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“…2). Regarding the apo-WT, l 0,0 was 410.4 6 0.1 nm, a value consistent with a slightly nonpolar site (411 nm) (40). The BW was relatively large (4.17 nm) compared to sites of a structurally homogeneous protein (i.e., BW # 2.11 nm of Rhodospirillum rubrum transhydrogenase (41)) and confirmed conformational heterogeneity in the Trp microenvironment.…”
Section: Steady-state Fluorescence Spectroscopymentioning
confidence: 68%
“…2). Regarding the apo-WT, l 0,0 was 410.4 6 0.1 nm, a value consistent with a slightly nonpolar site (411 nm) (40). The BW was relatively large (4.17 nm) compared to sites of a structurally homogeneous protein (i.e., BW # 2.11 nm of Rhodospirillum rubrum transhydrogenase (41)) and confirmed conformational heterogeneity in the Trp microenvironment.…”
Section: Steady-state Fluorescence Spectroscopymentioning
confidence: 68%
“…The paucity of structural information on proteins in the frozen state is due primarily to the insensitivity or the poor resolution of ordinary spectroscopic methods, or both, in such a highly scattering and anisotropic medium as ice. We have overcome these limitations by employing the phosphorescence emission of tryptophan (Trp) residues as a monitor of the polypeptide dynamical structure; this is an intrinsic probe that has been instrumental in disclosing conformational changes of proteins in response to variations in conditions of the medium (Strambini and Gabellieri, 1984; Strambini and Gonnelli, 1988; Cioni and Strambini, 1994) or elicited by the binding of substrate and effector molecules (Galley and Strambini, 1976;Cioni and Strambini, 1989;Strambini and Gonnelli, 1990;Strambini et al, 1992). The proteins selected for this study, monomers, dimers, and tetramers, have known crystallographic structure and possess a sole Trp residue per subunit that exhibits a long-lived, room-temperature phosphorescence emission.…”
Section: Introductionmentioning
confidence: 99%
“…Indirect techniques are also suitable for measuring the binding properties of nonquenching ligands (e.g., 136-138). 366 Measurements of phosphorescence quenching 370,371 and delayed fluorescence 372 are alternative emission techniques for investigating the binding properties of CA. The low quantum yields of phosphorescence, due to intersystem crossing and to the requirement for cryogenic conditions, diminish the practical importance of methods involving the triplet excited state.…”
Section: Fluorescence and Luminescence Spectroscopymentioning
confidence: 99%