Published in FEBS J on December 01, 2005
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Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proc Natl Acad Sci U S A (2005) 1.31
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Trapping the on-pathway folding intermediate of Im7 at equilibrium. J Mol Biol (2004) 1.29
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Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design. J Mol Biol (2004) 1.23
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NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. J Mol Biol (2006) 1.17
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The N-terminal helix is a post-assembly clamp in the bacterial outer membrane protein PagP. J Mol Biol (2007) 1.13
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Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7. J Mol Biol (2004) 1.05
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Viscoelastic study of the mechanical unfolding of a protein by AFM. Biophys J (2006) 1.01
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Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. Proc Natl Acad Sci U S A (2010) 1.00
Separation of beta2-microglobulin conformers by high-field asymmetric waveform ion mobility spectrometry (FAIMS) coupled to electrospray ionisation mass spectrometry. Rapid Commun Mass Spectrom (2004) 0.99
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Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Eng Des Sel (2009) 0.96
Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J Biol Chem (2004) 0.96
The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9. J Mol Biol (2007) 0.95
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Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J Mol Biol (2013) 0.91
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Amyloid under the atomic force microscope. Protein Pept Lett (2006) 0.88
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The organization of aromatic side groups in an amyloid fibril probed by solid-state 2H and 19F NMR spectroscopy. J Am Chem Soc (2006) 0.87
Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors. J Biol Chem (2013) 0.87
Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity. J Mol Biol (2012) 0.87