title: Resonance assignment of an engineered amino-terminal domain of a major ampullate spider silk with neutralized charge cluster.
abstract: 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.
authors.affiliation: Lehrstuhl Biopolymere, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany. daniel.schaal@uni-bayreuth.de.|Forschungszentrum für Bio-Makromoleküle (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany. daniel.schaal@uni-bayreuth.de.
authors.forename: Daniel
authors.initials: D
authors.lastname: Schaal
authors.affiliation: Lehrstuhl Biomaterialien, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.
authors.forename: Joschka
authors.initials: J
authors.lastname: Bauer
authors.affiliation: Lehrstuhl Biopolymere, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Forschungszentrum für Bio-Makromoleküle (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.
authors.forename: Kristian
authors.initials: K
authors.lastname: Schweimer
authors.affiliation: Lehrstuhl Biomaterialien, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Forschungszentrum für Bio-Makromoleküle (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Bayreuther Materialzentrum (BayMat), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.
authors.forename: Thomas
authors.initials: T
authors.lastname: Scheibel
authors.affiliation: Lehrstuhl Biopolymere, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Forschungszentrum für Bio-Makromoleküle (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.
authors.forename: Paul
authors.initials: P
authors.lastname: Rösch
authors.affiliation: Lehrstuhl Biopolymere, Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.|Forschungszentrum für Bio-Makromoleküle (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95447, Bayreuth, Germany.
authors.forename: Stephan
authors.initials: S
authors.lastname: Schwarzinger
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019906:Nuclear Magnetic Resonance, Biomolecular; D015202:Protein Engineering; D047011:Silk / Q000737:chemistry* / Q000235:genetics; D013112:Spiders / Q000737:chemistry*
chemical_list: D047011:Silk
keywords: Acidic charge cluster; Amino-terminal domain; Dimerization; Latrodectus hesperus; Major ampullate spidroin 1; Spider silk