Applications of 31P nuclear magnetic resonance to studies of protein structure and function

1983 ◽  
Vol 61 (4) ◽  
pp. 155-164 ◽  
Author(s):  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Alkaline Phosphatase ◽  
Protein Structure ◽  
Magnetic Resonance ◽  
Glycogen Phosphorylase ◽  
Structure And Function ◽  
Resonance Spectroscopy ◽  
Protein Structure And Function ◽  
And Function ◽  
Nuclear Magnetic

Selective illustrative applications of phosphorus-31 nuclear magnetic resonance spectroscopy to the study of protein structure and function are reviewed, including the enzymes alkaline phosphatase, myosin, actin, and glycogen phosphorylase.

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.

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