2H35
Solution structure of Human normal adult hemoglobin
Summary for 2H35
| Entry DOI | 10.2210/pdb2h35/pdb |
| Descriptor | Hemoglobin alpha subunit, Hemoglobin beta subunit, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | hemoglobin, hbco a, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64547.05 |
| Authors | |
| Primary citation | Xu, Y.,Zheng, Y.,Fan, J.S.,Yang, D. A new strategy for structure determination of large proteins in solution without deuteration Nat.Methods, 3:931-937, 2006 Cited by PubMed Abstract: 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. PubMed: 17060917DOI: 10.1038/nmeth938 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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