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Literature DB >> 456587

Conformational change and self association of monomeric melittin.

J C Talbot, J Dufourcq, J de Bony, J F Faucon, C Lussan.

Abstract

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Year: 1979 PMID： 456587 DOI： 10.1016/0014-5793(79)80957-6

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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41 in total

1. The virucidal EB peptide protects host cells from herpes simplex virus type 1 infection in the presence of serum albumin and aggregates proteins in a detergent-like manner.

Authors: Hermann Bultmann; Gary Girdaukas; Glen S Kwon; Curtis R Brandt
Journal: Antimicrob Agents Chemother Date: 2010-07-19 Impact factor: 5.191

2. Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature.

Authors: Shuichi Toraya; Takashi Nagao; Kazushi Norisada; Satoru Tuzi; Hazime Saitô; Shunsuke Izumi; Akira Naito
Journal: Biophys J Date: 2005-08-19 Impact factor: 4.033

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

Authors: M Smoluch; M Gorseling; C Gooijer; G van der Zwan
Journal: J Fluoresc Date: 2004-01 Impact factor: 2.217

4. Effect of permethylation on the haemolytic activity of melittin.

Authors: K Ramalingam; J Bello
Journal: Biochem J Date: 1992-06-15 Impact factor: 3.857

5. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions.

Authors: Laura H Lucas; Baran A Ersoy; Lisa A Kueltzo; Sangeeta B Joshi; Duane T Brandau; Nagarajan Thyagarajapuram; Laura J Peek; C Russell Middaugh
Journal: Protein Sci Date: 2006-09-08 Impact factor: 6.725

Conformational change and self association of monomeric melittin.

1. The virucidal EB peptide protects host cells from herpes simplex virus type 1 infection in the presence of serum albumin and aggregates proteins in a detergent-like manner.

2. Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature.

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

4. Effect of permethylation on the haemolytic activity of melittin.

5. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions.

6. Does dimeric melittin occur in aqueous solutions?

7. Nature of melittin-phospholipid interaction.

8. Solid-state NMR structure determination of melittin in a lipid environment.

9. Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR.

10. Action of melittin on the DPPC-cholesterol liquid-ordered phase: a solid state 2H-and 31P-NMR study.