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F. Hagn, Lukas Eisoldt, J. Hardy, C. Vendrely, M. Coles, T. Scheibel, H. Kessler (2010)
A conserved spider silk domain acts as a molecular switch that controls fibre assemblyNature, 465
Gefei Chen, Xiangqin Liu, Yunlong Zhang, Senzhu Lin, Zijiang Yang, J. Johansson, A. Rising, Qing Meng (2012)
Full-Length Minor Ampullate Spidroin Gene SequencePLoS ONE, 7
N. Kronqvist, M. Otikovs, Volodymyr Chmyrov, Gefei Chen, M. Andersson, K. Nordling, M. Landreh, M. Sarr, H. Jörnvall, S. Wennmalm, J. Widengren, Qing Meng, A. Rising, D. Otzen, S. Knight, K. Jaudzems, J. Johansson (2014)
Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formationNature Communications, 5
M. Landreh, G. Askarieh, K. Nordling, M. Hedhammar, A. Rising, C. Casals, J. Astorga-Wells, G. Alvélius, S. Knight, J. Johansson, H. Jörnvall, T. Bergman (2010)
A pH-dependent dimer lock in spider silk protein.Journal of molecular biology, 404 2
M. Sattler, J. Schleucher, C. Griesinger (1999)
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradientsProgress in Nuclear Magnetic Resonance Spectroscopy, 34
W. Vranken, W. Boucher, T. Stevens, R. Fogh, A. Pajon, M. Llinás, E. Ulrich, J. Markley, J. Ionides, E. Laue (2005)
The CCPN data model for NMR spectroscopy: Development of a software pipelineProteins: Structure, 59
M Sattler, J Schleucher, C Griesinger (1999)
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution empolying pulsed field gradientsProg NMR Spectrosc, 34
G. Askarieh, M. Hedhammar, K. Nordling, A. Sáenz, C. Casals, A. Rising, J. Johansson, S. Knight (2010)
Self-assembly of spider silk proteins is controlled by a pH-sensitive relayNature, 465
E. Bini, D. Knight, D. Kaplan (2004)
Mapping domain structures in silks from insects and spiders related to protein assembly.Journal of molecular biology, 335 1
E. Zuiderweg, S. Fesik (1989)
Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a.Biochemistry, 28 6
W. Gaines, Michael Sehorn, W. Marcotte (2010)
Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly*The Journal of Biological Chemistry, 285
Ming Xu, R. Lewis (1990)
Structure of a protein superfiber: spider dragline silk.Proceedings of the National Academy of Sciences of the United States of America, 87
S. Mori, C. Abeygunawardana, M. Johnson, P. Vanzijl (1995)
Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation.Journal of magnetic resonance. Series B, 108 1
Mike Hinman, R. Lewis (1992)
Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.The Journal of biological chemistry, 267 27
D. Marion, P. Driscoll, L. Kay, P. Wingfield, A. Bax, A. Gronenborn, G. Clore (1989)
Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta.Biochemistry, 28 15
A. Rising, G. Hjälm,, W. Engström, J. Johansson (2006)
N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins.Biomacromolecules, 7 11
Jessica Garb, Nadia Ayoub, C. Hayashi (2010)
Untangling spider silk evolution with spidroin terminal domainsBMC Evolutionary Biology, 10
F. Hagn, Christopher Thamm, T. Scheibel, H. Kessler (2011)
pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation.Angewandte Chemie, 50 1
Yang Shen, A. Bax (2013)
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networksJournal of Biomolecular NMR, 56
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.
Biomolecular NMR Assignments – Springer Journals
Published: Feb 19, 2016
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