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 Polypeptide Backbone Conformation of the E.*coli Outer Membrane Protein W
NMR Polypeptide Backbone Conformation of the E.*coli Outer Membrane Protein W
Publication date: Available online 10 July 2014
Source:Structure</br>
Author(s): Reto Horst , Pawel Stanczak , Kurt Wüthrich</br>
The outer membrane proteins (Omps) are key factors for bacterial survival and virulence. Among the Omps that have been structurally characterized either by X-ray crystallography or by NMR in solution, the crystal structure of OmpW stands out because three of its four extracellular loops are well defined, whereas long extracellular loops in other E.*coli Omps...
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07-10-2014 08:28 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, 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
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05-08-2014 05:38 PM
[NMR paper] High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
Related Articles High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
PLoS One. 2013;8(10):e78116
Authors: Zook JD, Molugu TR, Jacobsen NE, Lin G, Soll J, Cherry BR, Brown MF, Fromme P
Abstract
Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our...
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11-11-2013 01:30 AM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
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03-02-2011 02:01 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...