2h35

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[[Image:2h35.gif|left|200px]]<br />
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[[Image:2h35.gif|left|200px]]<br /><applet load="2h35" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2h35" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2h35" />
caption="2h35" />
'''Solution structure of Human normal adult hemoglobin'''<br />
'''Solution structure of Human normal adult hemoglobin'''<br />
==Overview==
==Overview==
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So far high-resolution structure determination by nuclear magnetic, resonance (NMR) spectroscopy has been limited to proteins &lt;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.
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So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins &lt;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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2H35 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H35 OCA].
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2H35 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H35 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fan, J.S.]]
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[[Category: Fan, J S.]]
[[Category: Yang, D.]]
[[Category: Yang, D.]]
[[Category: HEC]]
[[Category: HEC]]
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[[Category: hemoglobin]]
[[Category: hemoglobin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:25:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:41 2008''

Revision as of 15:37, 21 February 2008


2h35

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Solution structure of Human normal adult hemoglobin

Contents

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.

Disease

Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]

About this Structure

2H35 is a Protein complex structure of sequences from Homo sapiens with as ligand. 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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