Two-step self-assembly of a spider silk molecular clamp

[1]  Thomas H. Clarke,et al.  Genomic perspectives of spider silk genes through target capture sequencing: Conservation of stabilization mechanisms and homology-based structural models of spidroin terminal regions. , 2018, International journal of biological macromolecules.

[2]  Torsten Schwede,et al.  SWISS-MODEL: homology modelling of protein structures and complexes , 2018, Nucleic Acids Res..

[3]  M. Řezáč,et al.  Conservation of a pH-sensitive structure in the C-terminal region of spider silk extends across the entire silk gene family , 2018, Heredity.

[4]  Antonino Ingargiola,et al.  Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer , 2018, Science.

[5]  Christopher M Johnson,et al.  Conservation of folding and association within a family of spidroin N-terminal domains , 2017, Scientific Reports.

[6]  T. Scheibel,et al.  Conformational Stability and Interplay of Helical N- and C-Terminal Domains with Implications on Major Ampullate Spidroin Assembly. , 2017, Biomacromolecules.

[7]  Antonio Suma,et al.  How to fold intricately: using theory and experiments to unravel the properties of knotted proteins. , 2016, Current opinion in structural biology.

[8]  Cristian Micheletti,et al.  How to fold intricately: using theory and experiments to unravel the properties of knotted proteins , 2016, bioRxiv.

[9]  Matthias Rief,et al.  Knotting and unknotting of a protein in single molecule experiments , 2016, Proceedings of the National Academy of Sciences.

[10]  Anna Rising,et al.  Toward spinning artificial spider silk. , 2015, Nature chemical biology.

[11]  Katherine Bourzac,et al.  Spiders: Web of intrigue , 2015, Nature.

[12]  Sophie E Jackson,et al.  Mechanistic insights into the folding of knotted proteins in vitro and in vivo. , 2015, Journal of molecular biology.

[13]  Hannes Neuweiler,et al.  Microsecond folding and domain motions of a spider silk protein structural switch. , 2014, Journal of the American Chemical Society.

[14]  S. Gagné,et al.  Effect of pH on the structure of the recombinant C-terminal domain of Nephila clavipes dragline silk protein. , 2014, Biomacromolecules.

[15]  J. Johansson,et al.  Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains , 2014, PLoS biology.

[16]  Jerker Widengren,et al.  Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation , 2014, Nature Communications.

[17]  Daiwen Yang,et al.  Structure and function of C-terminal domain of aciniform spidroin. , 2014, Biomacromolecules.

[18]  Hannes Neuweiler,et al.  The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening , 2013, Nature Communications.

[19]  Daiwen Yang,et al.  Structural Characterization of Minor Ampullate Spidroin Domains and Their Distinct Roles in Fibroin Solubility and Fiber Formation , 2013, PloS one.

[20]  Hans Jörnvall,et al.  pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain. , 2012, Journal of molecular biology.

[21]  Thomas Scheibel,et al.  The role of terminal domains during storage and assembly of spider silk proteins , 2012, Biopolymers.

[22]  Y. Hsia,et al.  Conserved C-terminal domain of spider tubuliform spidroin 1 contributes to extensibility in synthetic fibers. , 2012, Biomacromolecules.

[23]  Thomas Scheibel,et al.  pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation. , 2011, Angewandte Chemie.

[24]  A. Fersht,et al.  Kinetics of chain motions within a protein-folding intermediate , 2010, Proceedings of the National Academy of Sciences.

[25]  Lukasz Goldschmidt,et al.  Structure and folding of a designed knotted protein , 2010, Proceedings of the National Academy of Sciences.

[26]  Michael G. Sehorn,et al.  Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly* , 2010, The Journal of Biological Chemistry.

[27]  Anna Rising,et al.  Self-assembly of spider silk proteins is controlled by a pH-sensitive relay , 2010, Nature.

[28]  Thomas Scheibel,et al.  A conserved spider silk domain acts as a molecular switch that controls fibre assembly , 2010, Nature.

[29]  Thomas Scheibel,et al.  Spider silk: from soluble protein to extraordinary fiber. , 2009, Angewandte Chemie.

[30]  Huan‐Xiang Zhou,et al.  Fundamental aspects of protein-protein association kinetics. , 2009, Chemical reviews.

[31]  Z. Shao,et al.  Elasticity of spider silks. , 2008, Biomacromolecules.

[32]  B. Bowler.  Thermodynamics of protein denatured states. , 2007, Molecular bioSystems.

[33]  Sophie E. Jackson,et al.  The Dimerization of an α/β-Knotted Protein Is Essential for Structure and Function , 2007 .

[34]  Anna L. Mallam,et al.  The dimerization of an alpha/beta-knotted protein is essential for structure and function. , 2007, Structure.

[35]  S. Goodacre,et al.  Evolution of spider silks: conservation and diversification of the C‐terminus , 2006, Insect molecular biology.

[36]  Sophie E Jackson,et al.  Folding studies on a knotted protein. , 2005, Journal of molecular biology.

[37]  J. Hofrichter,et al.  The protein folding 'speed limit'. , 2004, Current opinion in structural biology.

[38]  D. Baker,et al.  Realistic protein–protein association rates from a simple diffusional model neglecting long‐range interactions, free energy barriers, and landscape ruggedness , 2004, Protein science : a publication of the Protein Society.

[39]  H. Grubmüller,et al.  Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1 , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[40]  W. Colón,et al.  From two-state to three-state: the effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism. , 2002, Biochemistry.

[41]  Fritz Vollrath,et al.  Liquid crystalline spinning of spider silk , 2001, Nature.

[42]  M. Cromwell,et al.  Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. , 1999, Biochemistry.

[43]  S. Jackson,et al.  How do small single-domain proteins fold? , 1998, Folding & design.

[44]  R. Lewis,et al.  Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks. , 1998, Journal of molecular biology.

[45]  J. Janin.  The kinetics of protein‐protein recognition , 1997, Proteins.

[46]  B. Packard,et al.  Profluorescent protease substrates: intramolecular dimers described by the exciton model. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[47]  A. Fink,et al.  Classification of acid denaturation of proteins: intermediates and unfolded states. , 1994, Biochemistry.

[48]  Daniela Fischer,et al.  Web of intrigue , 1993, Nature.

[49]  A. Fersht,et al.  Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. , 1991, Biochemistry.

[50]  R. Lewis,et al.  Molecular mechanism of spider silk elasticity. , 1991, Archives of biochemistry and biophysics.

[51]  D. W. Bolen,et al.  Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. , 1988, Biochemistry.

[52]  D. W. Bolen,et al.  Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. , 1988, Biochemistry.

[53]  M. Volkenstein,et al.  Statistical mechanics of chain molecules , 1970 .

[54]  C. Tanford.  Protein denaturation. , 1968, Advances in protein chemistry.

[55]  P. Flory,et al.  The Configuration of Random Polypeptide Chains. II. Theory , 1965 .