Protein tryptophan accessibility studied by fluorescence quenching

@article{Mller2002ProteinTA,
  title={Protein tryptophan accessibility studied by fluorescence quenching},
  author={Matias N. M{\"o}ller and Ana Denicola},
  journal={Biochemistry and Molecular Biology Education},
  year={2002},
  volume={30}
}
  • M. Möller, A. Denicola
  • Published 1 May 2002
  • Physics, Chemistry
  • Biochemistry and Molecular Biology Education
A laboratory class is described to introduce the biochemistry major students to the basic concepts and various applications of fluorescence spectroscopy. Through simple and inexpensive experiments the students learn how to record excitation and emission spectra and measure intrinsic protein fluorescence and its quenching to elucidate the local tryptophan environment. Free tryptophan, ovalbumin, and bovine serum albumin are used for the experiments. The structural information that can be… 
Study of protein‐ligand binding by fluorescence
TLDR
The major aim is to introduce the students to the basic concepts of fluorescence emission (intrinsic and extrinsic), the effect of environment on fluorescence parameters, and how this could be applied to the study of ligand binding to proteins.
Tryptophan Fluorescence Quenching Assays for Measuring Protein-ligand Binding Affinities: Principles and a Practical Guide.
TLDR
This protocol describes how to use tryptophan fluorescence quenching to investigate the binding affinity of a protein for its partner/ligand and how to check and correct for the inner filter effect.
A project‐based biochemistry laboratory promoting the understanding and uses of fluorescence spectroscopy in the study of biomolecular structures and interactions
  • N. Briese, H. Jakubowski
  • Chemistry
    Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology
  • 2007
A laboratory project for a first semester biochemistry course is described, which integrates the traditional classroom study of the structure and function of biomolecules with the laboratory study of
Tryptophan fluorescence quenching as a binding assay to monitor protein conformation changes in the membrane of intact mitochondria
Intrinsic protein fluorescence is due to aromatic amino acids, mainly tryptophan, which can be selectively measured by exciting at 295 nm. Changes in emission spectra of tryptophan are due to the
Mechanism for Fluorescence Quenching of Tryptophan by Oxamate and Pyruvate: Conjugation and Solvation-Induced Photoinduced Electron Transfer.
TLDR
To find the mechanism of the quenching by oxamate and pyruvate, density functional theory computations with a polarizable continuum model, solvation based on density, and explicit waters, indicate that both molecules can be an electron acceptor via photoinduced electron transfer.
Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
The main objective of this research was to explore the fluorescence quenching mechanism of a humic substance (Suwannee River natural organic matter (SWNOM)) to amino acids (tryptophan, tyrosine)
...
...

References

SHOWING 1-10 OF 11 REFERENCES
Principles of fluorescence spectroscopy
TLDR
This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion.
TLDR
The results of the model compound study provide evidence for a mechanism that follows the classical Stern-Volmer law (1919), predominantly involving collisional quenching, and illustrate the importance of local charge and solvent viscosity.
Topics in fluorescence spectroscopy
Topics in fluorescence spectroscopy , Topics in fluorescence spectroscopy , مرکز فناوری اطلاعات و اطلاع رسانی کشاورزی
Bovine Mercaptalbumin and Non-mercaptalbumin Monomers INTERCONVERSIONS AND STRUCTURAL DIFFERENCES
TLDR
Studies with undefatted and defatted monomers indicate that one of the primary fatty acid binding sites is also located in this part of the crevice and that oxidation of the cysteinyl sulfhydryl group alters the binding of fatty acid at this site.
Bovine Mercaptalbumin and Non-mercaptalbumin Monomers
Determination of serum proteins by means of the biuret reaction.
Solute quenching of protein fluorescence.
Solute perturbation of protein fluorescence
  • The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion , Biochemistry
  • 1971
...
...