Resonance assignment of an engineered amino-terminal domain of a major ampullate spider silk with neutralized charge cluster
Title data
Schaal, Daniel ; Bauer, Joschka ; Schweimer, Kristian ; Scheibel, Thomas ; Rösch, Paul ; Schwarzinger, Stephan: Resonance assignment of an engineered amino-terminal domain of a major ampullate spider silk with neutralized charge cluster. In: Biomolecular NMR Assignments.
Vol. 10
(2016)
.
- pp. 199-202.
ISSN 1874-270X
DOI: https://doi.org/10.1007/s12104-016-9666-y
Abstract in another language
Spider dragline fibers are predominantly made out of the major ampullate spidroins (MaSp) 1 and 2. The assembly of dissolved spidroin into a stable fiber is highly controlled for example by dimerization of its amino-terminal domain (NRN) upon acidification, as well as removal of sodium chloride along the spinning duct. Clustered residues D39, E76 and E81 are the most highly conserved residues of the five-helix bundle, and they are hypothesized to be key residues for switching between a monomeric and a dimeric conformation. Simultaneous replacement of these residues by their non-titratable analogues results in variant D39N/E76Q/E81Q, which is supposed to fold into an intermediate conformation between that of the monomeric and the dimeric state at neutral pH. Here we report the resonance assignment of Latrodectus hesperus NRN variant D39N/E76Q/E81Q at pH 7.2 obtained by high-resolution triple resonance NMR spectroscopy
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