scholarly journals Rheology and nuclear magnetic resonance measurements under shear of sodium dodecyl sulfate/decanol/water nematics

2001 ◽  
Vol 45 (1) ◽  
pp. 29-48 ◽  
Author(s):  
Thomas Thiele ◽  
J.-F. Berret ◽  
Stefan Müller ◽  
Claudia Schmidt
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Dodecyl Sulfate ◽  
Nuclear Magnetic

scholarly journals Mutagenesis and Nuclear Magnetic Resonance Analyses of the Fusion Peptide of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein

2008 ◽  
Vol 82 (16) ◽  
pp. 8138-8148 ◽  
Author(s):  
Ying Tan ◽  
Ling Jiang ◽  
Manli Wang ◽  
Feifei Yin ◽  
Fei Deng ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Helicoverpa Armigera ◽  
Sodium Dodecyl ◽  
Fusion Peptide ◽  
Structure And Function ◽  
F Protein ◽  
Helicoverpa Armígera ◽  
And Function ◽  
Nuclear Magnetic

ABSTRACT The entry of enveloped viruses into cells is normally mediated by fusion between viral and cellular membranes, in which the fusion peptide plays a crucial role. The fusion peptides of group II nucleopolyhedrovirus (NPV) F proteins are quite conserved, with a hydrophobic region located at the N terminal of the F1 fragment. For this report, we used mutagenesis and nuclear magnetic resonance (NMR) to study the structure and function of the fusion peptide of the Helicoverpa armigera single-nucleocapsid NPV (HearNPV) F protein (HaF). Five mutations in the fusion peptide of HaF, N1G, N1L, I2N, G3L, and D11L, were generated separately, and the mutated f genes were transformed into the f-null HearNPV bacmid. The mutations N1L, I2N, and D11L were found to completely abolish the ability of the recombinant bacmids to produce infectious budded virus, while the mutations N1G and G3L did not. The low-pH-induced envelope fusion assay demonstrated that the N1G substitution increased the fusogenicity of HaF, while the G3L substitution reduced its fusogenicity. NMR spectroscopy was used to determine the structure of a synthetic fusion peptide of HaF in the presence of sodium dodecyl sulfate micelles at pH 5.0. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N terminus from N1 to N5, a 310-helix from F6 to G8, a turn at S9, and a regular α-helix from V10 to D19. The data provide the first NMR structure of a baculovirus fusion peptide and allow us to further understand the relationship of structure and function of the fusion peptide.

Structure of the glycan chain from the surface layer glycoprotein of Bacillus alvei CCM 2051

1991 ◽  
Vol 69 (1) ◽  
pp. 72-78 ◽  
Author(s):  
Eleonora Altman ◽  
Jean-Robert Brisson ◽  
Paul Messner ◽  
Uwe B. Sleytr
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Surface Layer ◽  
Magnetic Resonance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Glycan Chain ◽  
Molecular Masses ◽  
Nuclear Magnetic

The cell surface of the mesophilic eubacterium Bacillus alvei CCM 2051 is covered by an oblique arranged surface layer glycoprotein. The subunits revealed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis were distinct bands of molecular masses 140 000, 128 000, and 127 000. Proteolytic degradation of the purified S-layer glycoprotein yielded a single glycopeptide fraction with an apparent molecular mass of ca. 25 000. Methylation analysis in conjunction with two-dimensional nuclear magnetic resonance experiments at 500 MHz established the branched trisaccharide[Formula: see text]as the repeating unit for this glycan chain.Key words: surface layer, eubacteria, glycoprotein, nuclear magnetic resonance, structure.

Sign in / Sign up

Export Citation Format

Share Document