ArticleBiophysical journal2003
The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 48 citations in OpenAlex.
- Advanced Spectroscopy and APBS Modeling for Determination of the Role of His190 and Trp103 in Mouse Thymidylate Synthase Interaction with Selected dUMP Analogues.International journal of molecular sciences · 2021Article
- Comparison of tryptophan fluorescence lifetimes in cyanobacterial photosystem I frozen in the light and in the dark.Photosynthesis research · 2019Article
- The broken ring: reduced aromaticity in Lys-Trp cations and high pH tautomer correlates with lower quantum yield and shorter lifetimes.The journal of physical chemistry. B · 2014Article
- Tryptophan conformations associated with partial unfolding in ribonuclease T1.Biophysical journal · 2009Article
- Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.Biophysical journal · 2008Article
- An unusual red-edge excitation and time-dependent Stokes shift in the single tryptophan mutant protein DD-carboxypeptidase from Streptomyces: the role of dynamics and tryptophan rotamers.Protein science : a publication of the Protein Society · 2008Article
- Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling.Biophysical journal · 2006Article
- Study of the interaction between Apis mellifera venom and micro-heterogeneous systems.Journal of fluorescence · 2006Article
- Protein simulations: the absorption spectrum of barnase point mutants.Protein science : a publication of the Protein Society · 2004Article
- Conformational effects on tryptophan fluorescence in cyclic hexapeptides.Biophysical journal · 2004Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Dead-End Elimination method was used to identify 40 low energy microconformations of 16 tryptophan residues in eight proteins. Single Trp-mutants of these proteins all show a double- or triple-exponential fluorescence decay. For ten of these lifetimes the corresponding rotameric state could be identified by comparing the bimolecular acrylamide quenching constant (k(q)) and the relative solvent exposure of the side chain in that microstate. In the absence of any identifiable quencher, the origin of the lifetime heterogeneity is interpreted in terms of the electron transfer process from the indole C epsilon 3 atom to the carbonyl carbon of the peptide bond. Therefore it is expected that a shorter [C epsilon 3-C[double bond]O] distance leads to a shorter lifetime as observed for these ten rotamers. Applying the same rule to the other 30 lifetimes, a link with their corresponding rotameric state could also be made. In agreement with the theory of Marcus and Sutin, the nonradiative rate constant shows an exponential relationship with the [C epsilon 3-C[double bond]O] distance for the 40 datapoints.
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