2h25
From Proteopedia
(New page: 200px<br /><applet load="2h25" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h25" /> '''Solution Structure of Maltose Binding Protei...) |
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'''Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin'''<br /> | '''Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | So far high-resolution structure determination by nuclear magnetic | + | So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins <30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling. |
==About this Structure== | ==About this Structure== | ||
| - | 2H25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 2H25 is a [http://en.wikipedia.org/wiki/Single_protein 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=2H25 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:28 2008'' |
Revision as of 15:37, 21 February 2008
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Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin
Overview
So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins <30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling.
About this Structure
2H25 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A new strategy for structure determination of large proteins in solution without deuteration., Xu Y, Zheng Y, Fan JS, Yang D, Nat Methods. 2006 Nov;3(11):931-7. PMID:17060917
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