Literature DB >> 15622858

Temperature dependence of the melittin folding equilibrium studied by means of fluorescence excitation spectra.

M Smoluch1, M Gorseling, C Gooijer, G van der Zwan.   

Abstract

The temperature dependence of fluorescence excitation spectra is investigated. This gives information on melittin folding equilibrium complementary to that obtained from fluorescence emission studies. A fit of the excitation spectra of melittin with three Gaussian functions gives good results. It suggests that in melittin a reversal of La and Lb electronic states of tryptophane takes place. The separate La and Lb bands exhibit a temperature dependence of the width and maximum.

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Year:  2004        PMID: 15622858     DOI: 10.1023/b:jofl.0000014657.97498.d1

Source DB:  PubMed          Journal:  J Fluoresc        ISSN: 1053-0509            Impact factor:   2.217


  11 in total

Review 1.  The red-edge effects: 30 years of exploration.

Authors:  Alexander P Demchenko
Journal:  Luminescence       Date:  2002 Jan-Feb       Impact factor: 2.464

Review 2.  1La and 1Lb transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins.

Authors:  P R Callis
Journal:  Methods Enzymol       Date:  1997       Impact factor: 1.600

3.  [Structural-dynamic properties of the tryptophan residue environment in melittin].

Authors:  A P Demchenko; A S Ladokhin; E G Kostrzhevskaia
Journal:  Mol Biol (Mosk)       Date:  1987 May-Jun

4.  The self-association of melittin and its binding to lipids: an intrinsic fluorescence polarization study.

Authors:  J F Faucon; J Dufourcq; C Lussan
Journal:  FEBS Lett       Date:  1979-06-01       Impact factor: 4.124

5.  Conformational change and self association of monomeric melittin.

Authors:  J C Talbot; J Dufourcq; J de Bony; J F Faucon; C Lussan
Journal:  FEBS Lett       Date:  1979-06-01       Impact factor: 4.124

6.  The structure of melittin. II. Interpretation of the structure.

Authors:  T C Terwilliger; D Eisenberg
Journal:  J Biol Chem       Date:  1982-06-10       Impact factor: 5.157

7.  The structure of melittin. I. Structure determination and partial refinement.

Authors:  T C Terwilliger; D Eisenberg
Journal:  J Biol Chem       Date:  1982-06-10       Impact factor: 5.157

8.  Conformational studies of anionic melittin analogues: effect of peptide concentration, pH, ionic strength, and temperature--models for protein folding and halophilic proteins.

Authors:  K Ramalingam; S Aimoto; J Bello
Journal:  Biopolymers       Date:  1992-08       Impact factor: 2.505

9.  Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding.

Authors:  W Wilcox; D Eisenberg
Journal:  Protein Sci       Date:  1992-05       Impact factor: 6.725

10.  Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction.

Authors:  S C Quay; C C Condie
Journal:  Biochemistry       Date:  1983-02-01       Impact factor: 3.162

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