2d21
From Proteopedia
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NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)
Overview
Nuclear-magnetic-resonance spectroscopy can determine the, three-dimensional structure of proteins in solution. However, its, potential has been limited by the difficulty of interpreting NMR spectra, in the presence of broadened and overlapping resonance lines and low, signal-to-noise ratios. Here we present stereo-array isotope labelling, (SAIL), a technique that can overcome many of these problems by applying a, complete stereospecific and regiospecific pattern of stable isotopes that, is optimal with regard to the quality and information content of the, resulting NMR spectra. SAIL uses exclusively chemically and enzymatically, synthesized amino acids for cell-free protein expression. We demonstrate, for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding, protein that SAIL offers sharpened lines, spectral simplification without, loss of information, and the ability to rapidly collect the structural, restraints required to solve a high-quality solution structure for, proteins twice as large as commonly solved by NMR. It thus makes a large, class of proteins newly accessible to detailed solution structure, determination.
About this Structure
2D21 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Optimal isotope labelling for NMR protein structure determinations., Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P, Nature. 2006 Mar 2;440(7080):52-7. PMID:16511487
Page seeded by OCA on Wed Nov 21 09:23:51 2007
