NDLI: Structure and coordination determination of peptide-metal complexes using 1D and 2D ¹H NMR.

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Year: 2013 Issue: 82

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Structure and coordination determination of peptide-metal complexes using 1D and 2D ¹H NMR.

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Structure and coordination determination of peptide-metal complexes using 1D and 2D ¹H NMR.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shoshan, Michal S. Tshuva, Edit Y. Shalev, Deborah E.
Description	Author Affiliation: Shoshan MS ( Department of Chemistry, The Hebrew University of Jerusalem.)
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 sequence MTCSGCSRPG (underlined is conserved), was determined in solution under inert conditions by NMR spectroscopy. NMR is a widely accepted technique for the determination of solution structures of proteins and peptides. Due to difficulty in crystallization to provide single crystals suitable for X-ray crystallography, the NMR technique is extremely valuable, especially as it provides information on the solution state rather than the solid state. Herein we describe all steps that are required for full three-dimensional structure determinations by NMR. The protocol includes sample preparation in an NMR tube, 1D and 2D data collection and processing, peak assignment and integration, molecular mechanics calculations, and structure analysis. Importantly, the analysis was first conducted without any preset metal-ligand bonds, to assure a reliable structure determination in an unbiased manner.
File Format	HTM / HTML
e-ISSN	1940087X
Journal	Journal of Visualized Experiments
Issue Number	82
Language	English
Publisher	MyJove Corp.
Publisher Date	2013-12-16
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physical Sciences Discipline Life Sciences Discipline Medicine Copper Chemistry Metallochaperones Nuclear Magnetic Resonance, Biomolecular Oligopeptides Cations, Monovalent Metabolism Protein Conformation Protons Research Support, Non-u.s. Gov't Video-audio Media
Content Type	Text
Resource Type	Article

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