ArticleBiophysical journal1999
Tryptophan rotamer distributions in amphipathic peptides at a lipid surface.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 55 citations in OpenAlex.
- Rotamer Dynamics: Analysis of Rotamers in Molecular Dynamics Simulations of Proteins.Biophysical journal · 2019Review
- Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement.European biophysics journal : EBJ · 2014Article
- 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
- Applications of phasor plots to in vitro protein studies.Analytical biochemistry · 2011Article
- Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin.Protein science : a publication of the Protein Society · 2010Article
- Ultrafast fluorescence spectroscopy via upconversion applications to biophysics.Methods in enzymology · 2008Review
- Interaction of an amphipathic peptide with phosphatidycholine/phosphatidylethanolamine mixed membranes.Biophysical journal · 2007Article
- Study of the interaction between Apis mellifera venom and micro-heterogeneous systems.Journal of fluorescence · 2006Article
- Conformational effects on tryptophan fluorescence in cyclic hexapeptides.Biophysical journal · 2004Article
- Interaction of the 18.5-kD isoform of myelin basic protein with Ca2+ -calmodulin: effects of deimination assessed by intrinsic Trp fluorescence spectroscopy, dynamic light scattering, and circular dichroism.Protein science : a publication of the Protein Society · 2003Article
- Solid-state 19F-NMR analysis of 19F-labeled tryptophan in gramicidin A in oriented membranes.Biophysical journal · 2002Article
- Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface.Biophysical journal · 2000Article
- A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data.Protein science : a publication of the Protein Society · 2000Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The fluorescence decay of tryptophan is a sensitive indicator of its local environment within a peptide or protein. We describe the use of frequency domain fluorescence spectroscopy to determine the conformational and environmental changes associated with the interaction of single tryptophan amphipathic peptides with a phospholipid surface. The five 18-residue peptides studied are based on a class A amphipathic peptide known to associate with lipid bilayers. The peptides contain a single tryptophan located at positions 2, 3, 7, 12, or 14 in the sequence. In aqueous solution, the peptides are unstructured and a triple-exponential function is required to fit the decay data. Association of the peptides with small unilamellar vesicles composed of egg phosphatidylcholine reduces the complexity of the fluorescence decays to a double exponential function, with a reduced dependence of the preexponential amplitude on peptide sequence. The data are interpreted in terms of a rotamer model in which the modality and relative proportions of the lifetime components are related to the population distribution of tryptophan chi1 rotamers about the Calpha-Cbeta bond. Peptide secondary structure and the disposition of the tryptophan residue relative to the lipid and aqueous phases in the peptide-lipid complex affect the local environment of tryptophan and influence the distribution of side-chain rotamers. The results show that measurement of the temporal decay of tryptophan emission provides a useful adjunct to other biophysical techniques for investigating peptide-lipid and protein-membrane interactions.
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