2h35

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(New page: 200px<br /> <applet load="2h35" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h35" /> '''Solution structure of Human normal adult he...)
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==Overview==
==Overview==
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.
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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==Disease==
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Known diseases associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Erythremias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Erythrocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], HPFH, deletion type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Heinz body anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Hemoglobin H disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Hypochromic microcytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Sickle cell anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemia, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Thalassemia-beta, dominant inclusion-body OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]]
==About this Structure==
==About this Structure==
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[[Category: hemoglobin]]
[[Category: hemoglobin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:31:03 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:25:39 2007''

Revision as of 20:19, 12 November 2007


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 HEC 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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