[NMR paper] Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion NMR Spectroscopy.
Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion NMR Spectroscopy.
Related Articles Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion NMR Spectroscopy.
Biochemistry. 2015 Jun 26;
Authors: Pustovalova Y, Kukic P, Vendruscolo M, Korzhnev DM
Abstract
The structural characterization of low-populated states of proteins with accuracy comparable to that achievable for native states is...
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06-27-2015 01:13 PM
[NMR paper] Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Biomol NMR Assign. 2013 Jul 14;
Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST
Abstract
YibK is a tRNA methyltransferase from Haemophilus influenzae, which forms a stable homodimer in solution and contains a deep trefoil 31 knot encompassing the C-terminal helix that threads through a long loop. It has been a model system for investigating knotted...
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07-16-2013 09:04 PM
[NMR paper] Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Biomol NMR Assign. 2013 Jul 3;
Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST
Abstract
YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent...
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07-05-2013 08:03 AM
[NMR paper] NMR characterization of residual structure in the denatured state of protein L.
NMR characterization of residual structure in the denatured state of protein L.
Related Articles NMR characterization of residual structure in the denatured state of protein L.
J Mol Biol. 2000 Jun 23;299(5):1341-51
Authors: Yi Q, Scalley-Kim ML, Alm EJ, Baker D
Triple-resonance NMR experiments were used to assign the (13)C(alpha), (13)C(beta), (15)N and NH resonances for all the residues in the denatured state of a destabilized protein L variant in 2 M guanidine. The chemical shifts of most resonances were very close to their random coil...
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11-18-2010 09:15 PM
[NMR paper] A comparison of the pH, urea, and temperature-denatured states of barnase by heteronu
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
J Mol Biol. 1995 Nov 24;254(2):305-21
Authors: Arcus VL, Vuilleumier S, Freund SM, Bycroft M, Fersht AR
The denatured states of...
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08-22-2010 03:50 AM
[NMR paper] NMR analysis of the residual structure in the denatured state of an unusual mutant of
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
Related Articles NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
Structure. 1993 Oct 15;1(2):121-34
Authors: Shortle D, Abeygunawardana C
BACKGROUND: Staphylococcal nuclease is a well-developed model system for analyzing the effects of mutations on protein folding and stability. Substitution of glycine 88 with valine (Gly88Val) destabilizes staphylococcal nuclease by 1.0...
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[NMR paper] NMR determination of residual structure in a urea-denatured protein, the 434-represso
NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Related Articles NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Science. 1992 Sep 11;257(5076):1559-63
Authors: Neri D, Billeter M, Wider G, Wüthrich K
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain...
NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor - Science
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