Related ArticlesAn Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Chembiochem. 2014 Feb 6;
Authors: Guan JY, Foerster JM, Drijfhout JW, Timmer M, Blok A, Ullmann GM, Ubbink M
Abstract
Protein complex formation involves an encounter state in which the proteins are associated in a nonspecific manner and often stabilized by interactions between charged surface patches. Such patches are thought to bind in many different orientations with similar affinity. To obtain experimental evidence for the dynamics in encounter complexes, a model was created using the electron transfer protein plastocyanin and short charged peptides. Three plastocyanins with distinct surface charge distributions were studied. The experimental results from chemical shift perturbations, paramagnetic relaxation enhancement (PRE) NMR, and theoretical results from Monte Carlo simulations indicate the presence of multiple binding orientations that interconvert quickly and are dominated by long-range charge interactions. The PRE data also suggest the presence of highly transient orientations stabilized by short-range interactions.
PMID: 24504673 [PubMed - as supplied by publisher]
[NMR paper] Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
Related Articles Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
J Vis Exp. 2013;(82)
Authors: Shoshan MS, Tshuva EY, Shalev DE
Abstract
Copper (I) binding by metallochaperone transport proteins prevents copper oxidation and release of the toxic ions that may participate in harmful redox reactions. The Cu (I) complex of the peptide model of a Cu (I) binding metallochaperone protein, which includes the...
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01-01-2014 03:05 PM
[NMR paper] NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
Angew Chem Int Ed Engl. 2013 Jul 19;
Authors: Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B
Abstract
Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome...
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07-23-2013 09:52 PM
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qcs9RnHBiBY
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09-08-2012 08:44 AM
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Abstract Carr-Purcell-Meiboom-Gill relaxation dispersion (CPMG RD) NMR spectroscopy has emerged as a powerful tool for quantifying the kinetics and thermodynamics of millisecond time-scale exchange processes involving the interconversion between a visible ground state and one or more minor, sparsely populated invisible â??excitedâ?? conformational states. Recently it has also become possible to determine atomic resolution...
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04-09-2012 01:19 AM
Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy
Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 58, Issues 1–2</br>
Cyril Dominguez, Mario Schubert, Olivier Duss, Sapna Ravindranathan, Frédéric H.-T. Allain</br>
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03-09-2012 09:16 AM
[NMR paper] Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly
Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin fragment.
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 Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin...
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08-22-2010 02:20 PM
[NMR paper] Protein complexes studied by NMR spectroscopy.
Protein complexes studied by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein complexes studied by NMR spectroscopy.
Curr Opin Biotechnol. 1996 Aug;7(4):403-8
Authors: Wand AJ, Englander SW
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point...
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[Question from NMRWiki Q&A forum] 2D pulse sequences for NMR of protein/peptide complexes?
2D pulse sequences for NMR of protein/peptide complexes?
Hello, I am looking for some 15N/13C-filtered 2D NOESY and 2D TOCSY pulse sequences to run on a Varian 600. Does anyone have any ideas where I would get some tried and tested pulse sequence input files?
Check if somebody has answered this question on NMRWiki QA forum
An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Linear Mode
