[NMR paper] Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Related Articles Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
J Am Chem Soc. 2014 Apr 16;
Authors: Huang JR, Warner LR, Sanchez C, Gabel F, Madl T, Mackereth CD, Sattler M, Blackledge M
Abstract
Multi-domain proteins containing intrinsically disordered linkers exhibit...
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[NMR paper] Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
J Am Chem Soc. 2013 Sep 30;
Authors: Marcelo F, Huecas S, Ruiz-Avila LB, Cañada FJ, Perona A, Poveda A, Martin-Santamaria S, Morreale A, Jimenez-Barbero J, Andreu JM
Abstract
FtsZ is the key protein of...
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[NMR paper] Exploration of the supramolecular interactions involving tris-dipicolinate lanthanide complexes in protein crystals by a combined biostructural, computational and NMR study.
Exploration of the supramolecular interactions involving tris-dipicolinate lanthanide complexes in protein crystals by a combined biostructural, computational and NMR study.
Related Articles Exploration of the supramolecular interactions involving tris-dipicolinate lanthanide complexes in protein crystals by a combined biostructural, computational and NMR study.
Phys Chem Chem Phys. 2013 Sep 24;
Authors: Dumont E, Pompidor G, D'Aléo A, Vicat J, Toupet L, Kahn R, Girard E, Maury O, Giraud N
Abstract
Incorporating in a non-covalent...
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Characterization of theConformational Equilibriumbetween the Two Major Substates of RNase A Using NMR Chemical Shifts
Characterization of theConformational Equilibriumbetween the Two Major Substates of RNase A Using NMR Chemical Shifts
Carlo Camilloni, Paul Robustelli, Alfonso De Simone, Andrea Cavalli and Michele Vendruscolo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210951z/aop/images/medium/ja-2011-10951z_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210951z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hzHeyLh4UmQ
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Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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Sequence-Dependent Enrichment of a Model Phosphopeptide: A Combined MALDI-TOF and NMR Study.
Sequence-Dependent Enrichment of a Model Phosphopeptide: A Combined MALDI-TOF and NMR Study.
Sequence-Dependent Enrichment of a Model Phosphopeptide: A Combined MALDI-TOF and NMR Study.
Anal Chem. 2011 Mar 23;
Authors: Lucre?ce M, Emmanuelle S, Fabienne B, Sandrine S, Olivier L, Ge?rard B
The goal of this study was to detect and quantify by MALDI-TOF MS the phosphorylation of a peptide containing the recognition motif of the Protein Kinase C (PKC). Such model peptide can be used as a phosphorylation probe to follow intracellular...
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03-25-2011 06:34 PM
[NMR paper] A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydro
A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
Biochemistry. 1996 Dec 24;35(51):16502-9
Authors: Sun ZY, Pratt EA, Simplaceanu V, Ho C
Partially folded protein intermediates have been observed by 19F-NMR spectroscopy during the equilibrium unfolding of the...
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[NMR paper] 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm w
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
Biochim Biophys Acta. 1990 Nov 15;1041(2):186-94
Authors: Hauksson JB, La Mar GN, Pande U, Pandey RK, Parish DW, Singh JP, Smith KM
The...