Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
From The DNP-NMR Blog:
Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
Singh, C., et al., Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy. The Journal of Physical Chemistry Letters, 2014. 5(22): p. 4044-4048.
http://dx.doi.org/10.1021/jz502081j
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11-24-2014 04:15 PM
[NMR paper] Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
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J Am Chem Soc. 2014 May 8;
Authors: Sanchez-Medina C, Sekhar A, Vallurupalli P, Cerminara M, Muñoz V, Kay LE
Abstract
The topographic features of the free energy landscapes that govern the thermodynamics and kinetics of conformational transitions in proteins, which in turn are integral for function, are not well understood....
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05-09-2014 07:01 PM
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Celia Sanchez-Medina, Ashok Sekhar, Pramodh Vallurupalli, Michele Cerminara, Victor Mun?oz and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja502705y/aop/images/medium/ja-2014-02705y_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja502705y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/uht26log5zQ
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05-08-2014 05:38 PM
[NMR paper] 19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
Biochemistry. 2013 Aug 1;
Authors: Kitevski-Leblanc JL, Hoang J, Thach W, Larda ST, Prosser RS
Abstract
While many proteins are recognized to undergo folding via an intermediate, the microscopic nature of folding intermediates is less understood. In this study, 19F NMR and near UV circular dichroism (CD) are used to characterize a transition to a thermal folding intermediate of calmodulin, a...
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08-04-2013 03:18 AM
[NMR paper] Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
J Phys Chem B. 2013 Jun 24;
Authors: Campos LA, Sadqi M, Liu J, Wang X, English DS, Munoz V
Abstract
Theory predicts that folding free energy landscapes are intrinsically malleable, and as such are expected to respond to perturbations in topographically complex...
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06-27-2013 01:52 AM
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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06-07-2011 11:05 AM
[NMR paper] Elucidation of the protein folding landscape by NMR.
Elucidation of the protein folding landscape by NMR.
Related Articles Elucidation of the protein folding landscape by NMR.
Methods Enzymol. 2005;394:299-321
Authors: Dyson HJ, Wright PE
NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in...
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11-24-2010 11:14 PM
[NMR paper] Intestinal fatty acid binding protein: the folding mechanism as determined by NMR stu
Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Related Articles Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Biochemistry. 2001 Jan 23;40(3):732-42
Authors: Hodsdon ME, Frieden C
The intestinal fatty acid binding protein is composed of two beta-sheets surrounding a large interior cavity. There is a small helical domain associated with the portal for entry of the ligand into the cavity. Denaturation of the protein has been monitored in a residue-specific...