[NMR paper] Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Biomol NMR Assign. 2019 Apr 02;:
Authors: Jones DNM, Wang J, Murphy EJ
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[NMR paper] NMR Chemical Shift Mapping of SH2 Peptide Interactions.
NMR Chemical Shift Mapping of SH2 Peptide Interactions.
Related Articles NMR Chemical Shift Mapping of SH2 Peptide Interactions.
Methods Mol Biol. 2017;1555:269-290
Authors: McKercher MA, Wuttke DS
Abstract
Heteronuclear single quantum coherence (HSQC) nuclear magnetic resonance (NMR) experiments offer a rapid and high resolution approach to gaining binding and conformational insights into a protein-peptide interaction. By tracking (1)H and (15)N chemical shift changes over the course of a peptide titration into isotopically...
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[NMR paper] Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
J Phys Chem B. 2016 Aug 29;
Authors: Toleikis Z, Sirotkin VA, Skvarnavi?ius G, Smirnovien? J, Roumestand C, Matulis D, Petrauskas V
Abstract
Human heat shock protein 90 (Hsp90) is a key...
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Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Juan C. Mun?oz-Garci?a, Eric Chabrol, Romain R. Vive?s, Aline Thomas, Jose? L. de Paz, Javier Rojo, Anne Imberty, Franck Fieschi, Pedro M. Nieto and Jesu?s Angulo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja511529x/20150319/images/medium/ja-2014-11529x_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja511529x...
[NMR paper] EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
J Biomol NMR. 2013 Sep 11;
Authors: Zuiderweg ER, Bagai I, Rossi P, Bertelsen EB
Abstract
For several of the proteins...
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[NMR paper] NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: cha
NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
Related Articles NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
J Mol Recognit. 2001 May-Jun;14(3):166-71
Authors: Song J, Markley JL
The substrate-like...
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[NMR paper] NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from t
NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
Protein Sci. 1997 Sep;6(9):1835-48
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Mapping the Complete Photocycle that Powers a Large Stokes Shift Red Fluorescent Protein
Linear Mode
