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OALib Journal期刊
ISSN: 2333-9721
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NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein
杆状病毒蛋白融合肽LdF在溶液中的NMR结构研究

Keywords: NMR,structure,2D NMR,fusion peptide of baculoviruse
核磁共振(NMR)
,结构,2D,NMR,杆状病毒融合肽

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Abstract:

LD130 is the fusion protein of baculoviruse Lymantria dispar multiple nucleopolyhedrovirus (LdMNPV). The N terminal conserved region of subunit F1 in LD130 is the fusion peptide, which actively induces membrane fusion processes. NMR methods were used to identify the solution structure of the fusion peptide under membrane simulated enviornment at low pH. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N-terminus, and a regular α-helix from L3 to V16. The structure of the LD130 fusion peptide allows us to further investigate the structure-functional relationship of the fusion peptide.

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