ArticleBiophysical journal2001
High-sensitivity fluorescence anisotropy detection of protein-folding events: application to alpha-lactalbumin.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- In-Vial Detection of Protein Denaturation Using Intrinsic Fluorescence Anisotropy.Analytical chemistry · 2023Article
- Fluorescence Anisotropy Studies on Bodipy (Pyrromethene 546) Dye as a Novel Thermal Probe.Journal of fluorescence · 2022Article
- Article
- Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Article
- Novel regulation of equlibrative nucleoside transporter 1 (ENT1) by receptor-stimulated Ca2+-dependent calmodulin binding.American journal of physiology. Cell physiology · 2016Article
- Micro-volume couette flow sample orientation for absorbance and fluorescence linear dichroism.Biophysical journal · 2004Article
- ENaC-membrane interactions: regulation of channel activity by membrane order.The Journal of general physiology · 2004Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An experimental procedure has been devised to record simultaneously fluorescence intensity and fluorescence anisotropy. A photoelastic modulator on the excitation beam enables the anisotropy signal to be recorded in one pass using a single photomultiplier tube and eliminates the need for a polarizer on the emission path. In conjunction with a stopped-flow mixer, providing a time-resolved capability, this procedure was used to study the refolding of apo alpha-lactalbumin following dilution from guanidinium chloride. Although the fluorescence intensity does not change detectably, the fluorescence anisotropy was found to resolve the conformational changes occurring between the initial unfolded state and the molten globule state formed either kinetically during refolding at pH 7.0 or at equilibrium at pH 2.0 (A-state). This result provides further evidence that fluorescence anisotropy is a valuable probe of protein structural transitions and that the information it provides concerning the rotational mobility of a fluorophore can be complementary to the information about the local environment provided by fluorescence intensity.
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Registered trials
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