2h35
From Proteopedia
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Solution structure of Human normal adult hemoglobin
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
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
Page seeded by OCA on Thu Nov 8 13:31:03 2007
Categories: Homo sapiens | Protein complex | Fan, J.S. | Yang, D. | HEC | Hbco a | Hemoglobin
