Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape
Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01153/20161214/images/medium/bi-2016-01153h_0016.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01153
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12-15-2016 06:49 PM
The Non-native Helical Intermediate State May Accumulateat Low pH in the Folding and Aggregation Landscape of the IntestinalFatty Acid Binding Protein
The Non-native Helical Intermediate State May Accumulateat Low pH in the Folding and Aggregation Landscape of the IntestinalFatty Acid Binding Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00390/20160803/images/medium/bi-2016-003902_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00390
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08-04-2016 11:21 PM
[NMR paper] Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Related Articles Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
ACS Chem Biol. 2016 May 24;
Authors: Unione L, Ortega G, Mallagaray A, Corzana F, Perez-Castells J, Canales A, Jimenez-Barbero J, Millet O
Abstract
Protein dynamics related to function can be nowadays structurally well characterized (i. e....
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05-25-2016 02:33 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.
Related Articles Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
J Am Chem Soc. 2014 May 8;
Authors: Sanchez-Medina C, Sekhar A, Vallurupalli P, Cerminara M, Muņoz 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
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[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] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
J Am Chem Soc. 2003 Oct 15;125(41):12432-42
Authors: Tolkatchev D, Xu P, Ni F
Protein-ligand interactions may lead to the formation of multiple...
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[NMR paper] Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei
Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
FEBS Lett. 1995 Mar 27;362(1):34-8
Authors: Weesie RJ, Askin D, Jansen FJ, de...
Mispacking and the Fitness Landscape of the GreenFluorescent Protein Chromophore Milieu
Linear Mode
