2d21
From Proteopedia
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| - | [[Image:2d21.gif|left|200px]] | + | [[Image:2d21.gif|left|200px]] |
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| - | '''NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)''' | + | {{Structure |
| + | |PDB= 2d21 |SIZE=350|CAPTION= <scene name='initialview01'>2d21</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2D21 is a [ | + | 2D21 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D21 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16511487 16511487] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: stereo-array isotope labelling]] | [[Category: stereo-array isotope labelling]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:21 2008'' |
Revision as of 14:22, 20 March 2008
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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 Thu Mar 20 16:22:21 2008
