ArticleProtein science : a publication of the Protein Society2000
A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 42 citations in OpenAlex.
- Dynamic Equilibrium between the Fluorescent State of Tryptophan and Its Cation-Electron Ion Pair Governs Triplet State Population.Journal of the American Chemical Society · 2025Article
- 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
- Combining Experimental Data and Computational Methods for the Non-Computer Specialist.Molecules (Basel, Switzerland) · 2020Review
- Protein dynamics control the progression and efficiency of the catalytic reaction cycle of the Escherichia coli DNA-repair enzyme AlkB.The Journal of biological chemistry · 2014Article
- Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling.Biophysical journal · 2006Article
- Single-spanning membrane protein insertion in membrane mimetic systems: role and localization of aromatic residues.European biophysics journal : EBJ · 2005Article
- Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.Biophysical journal · 2004Article
- Conformational effects on tryptophan fluorescence in cyclic hexapeptides.Biophysical journal · 2004Article
- The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.Biophysical journal · 2003Article
- Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm Nereis diversicolor upon Ca2+ or Mg2+ binding.Biophysical journal · 2003Article
- Tryptophan properties in fluorescence and functional stability of plasminogen activator inhibitor 1.Biophysical journal · 2003Article
- Conformational states of the switch I region of Ha-ras-p21 in hinge residue mutants studied by fluorescence lifetime and fluorescence anisotropy measurements.Protein science : a publication of the Protein Society · 2003Article
- Ca(2+) and membrane binding to annexin 3 modulate the structure and dynamics of its N terminus and domain III.Protein science : a publication of the Protein Society · 2002Article
- HIV-1 integrase catalytic core: molecular dynamics and simulated fluorescence decays.Biophysical journal · 2001Article
- Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease.Protein science : a publication of the Protein Society · 2000Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A method is presented that allows the calculation of the lifetimes of tryptophan residues on the basis of spectral and structural data. It is applied to two different proteins. The calcium binding protein from the sarcoplasm of the muscles of the sand worm Nereis diversicolor (NSCP) changes its conformation upon binding of Ca2+ or Mg2+. NSCP contains three tryptophan residues at position 4, 57, and 170, respectively. The fluorescence lifetimes of W57 are investigated in a mutant in which W4 and W170 have been replaced. The time resolved fluorescence properties of W57 are linked to its different microconformations, which were determined by a molecular dynamics simulation map. Together with the determination of the radiative rate constant from the wavelength of maximum intensity of the decay associated spectra, it was possible to determine an exponential relation between the nonradiative rate constant and the distance between the indole CE3 atom and the carbonyl carbon of the peptide bond reflecting a mechanism of electron transfer as the main determinant of the value for the nonradiative rate constant. This result allows the calculation of the fluorescence lifetimes from the protein structure and the spectra. This method was further tested for the tryptophan of Ha-ras p21 (W32) and for W43 of the Tet repressor, which resulted in acceptable values for the predicted lifetimes.
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