ArticleBiophysical journal2004
Conformational effects on tryptophan fluorescence in cyclic hexapeptides.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Selective Excitation of theACS omega · 2024Article
- 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
- Evaluating Iso-Mukaadial Acetate and Ursolic Acid Acetate asBiomolecules · 2019Article
- Polyubiquitin Drives the Molecular Interactions of the NF-κB Essential Modulator (NEMO) by Allosteric Regulation.The Journal of biological chemistry · 2015Article
- Tryptophan-to-heme electron transfer in ferrous myoglobins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Probing tertiary structure of proteins using single Trp mutations with circular dichroism at low temperature.The journal of physical chemistry. B · 2014Article
- Interaction of a synthetic antimicrobial peptide with model membrane by fluorescence spectroscopy.European biophysics journal : EBJ · 2013Article
- Article
- Tryptophan rotamer distribution revealed for the α-helix in tear lipocalin by site-directed tryptophan fluorescence.The journal of physical chemistry. B · 2012Article
- Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics.European biophysics journal : EBJ · 2011Article
- Excited protein states of human tear lipocalin for low- and high-affinity ligand binding revealed by functional AB loop motion.Biophysical chemistry · 2010Article
- Tryptophan in the pore of the mechanosensitive channel MscS: assessment of pore conformations by fluorescence spectroscopy.The Journal of biological chemistry · 2010Article
- Structural and dynamic properties of juxta-membrane segments of caveolin-1 and caveolin-2 at the membrane interface.European biophysics journal : EBJ · 2010Article
- Intracavitary ligand distribution in tear lipocalin by site-directed tryptophan fluorescence.Biochemistry · 2009Article
- Peptide sequence and conformation strongly influence tryptophan fluorescence.Biophysical journal · 2008Article
- Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.Biophysical journal · 2008Article
- Dissection of complex protein dynamics in human thioredoxin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Quenchers induce wavelength dependence on protein fluorescence lifetimes.Journal of fluorescence · 2006Article
- Study of the interaction between Apis mellifera venom and micro-heterogeneous systems.Journal of fluorescence · 2006Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peptide bond quenches tryptophan fluorescence by excited-state electron transfer, which probably accounts for most of the variation in fluorescence intensity of peptides and proteins. A series of seven peptides was designed with a single tryptophan, identical amino acid composition, and peptide bond as the only known quenching group. The solution structure and side-chain chi(1) rotamer populations of the peptides were determined by one-dimensional and two-dimensional (1)H-NMR. All peptides have a single backbone conformation. The -, psi-angles and chi(1) rotamer populations of tryptophan vary with position in the sequence. The peptides have fluorescence emission maxima of 350-355 nm, quantum yields of 0.04-0.24, and triple exponential fluorescence decays with lifetimes of 4.4-6.6, 1.4-3.2, and 0.2-1.0 ns at 5 degrees C. Lifetimes were correlated with ground-state conformers in six peptides by assigning the major lifetime component to the major NMR-determined chi(1) rotamer. In five peptides the chi(1) = -60 degrees rotamer of tryptophan has lifetimes of 2.7-5.5 ns, depending on local backbone conformation. In one peptide the chi(1) = 180 degrees rotamer has a 0.5-ns lifetime. This series of small peptides vividly demonstrates the dominant role of peptide bond quenching in tryptophan fluorescence.
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