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Revisiting time-resolved protein phosphorescence.

Andrew R Draganski1, Maria G Corradini, Richard D Ludescher

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Summary
This summary is machine-generated.

Analyzing protein phosphorescence requires careful consideration of tyrosine emission, especially at low temperatures. New methods accurately separate tryptophan and tyrosine signals for precise protein analysis.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Spectroscopy

Background:

  • Time-resolved phosphorescence analysis of proteins can be complicated by interfering emission signals.
  • Tyrosine and solvent impurities can confound early decay data, particularly at colder temperatures.
  • Accurate analysis necessitates distinguishing tryptophan emission from other species like tyrosine.

Purpose of the Study:

  • To demonstrate the necessity of accounting for tyrosine emission in protein phosphorescence analysis.
  • To develop and present robust fitting procedures for resolving complex phosphorescence decay profiles.
  • To provide methods for separating tryptophan and tyrosine emission components in protein samples.

Main Methods:

  • Analysis of phosphorescence from simple mixtures of tryptophan and tyrosine in a glycerol-water solvent.
  • Development of two fitting procedures: maximum entropy method (MEM)-derived lifetime distribution and stretched exponential function.
  • Utilizing prior information from free-tryptophan decay curves at various temperatures to guide component separation.

Main Results:

  • Tyrosine emission is significant at low temperatures (below 185 K) and diminishes at higher temperatures.
  • Two distinct fitting procedures were successfully developed to resolve bimodal emission from proteins with both tryptophan and tyrosine residues.
  • The proposed methods effectively separate tryptophan phosphorescence from tyrosine interference.

Conclusions:

  • Accounting for tyrosine emission is crucial for accurate time-resolved phosphorescence analysis of proteins.
  • The developed fitting procedures offer reliable methods for deconvoluting complex phosphorescence signals.
  • These methods enhance the precision of studying tryptophan phosphorescence in proteins, especially in the presence of tyrosine.