Abstract
Sequence-specific assignment of the methyl groups in large proteins can be obtained from an MQ-(H)CC m H m -TOCSY experiment on uniformly 13C-labeled proteins without deuteration (Yang etal., 2004). Here the procedure is further demonstrated on a uniformly 13C-labeled α-chain or β-chain of human normal adult hemoglobin (65kDa) in the carbonmonoxy form. In addition, a strategy is presented for assigning protons of methyl-containing residues of uniformly 13C-labeled large proteins, on the basis of prior methyl assignments based on MQ-(H)CCH-TOCSY and H(C)C m H m -TOCSY experiments. Assignment of about 80% of the side-chain resonances of methyl-containing residues of carbonmonoxyhemoglobin has been obtained.
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Zheng, Y., Giovannelli, J.L., Ho, N.T. et al. Side-chain assignments of methyl-containing residues in a uniformly 13C-labeled hemoglobin in the carbonmonoxy form. J Biomol NMR 30, 423–429 (2004). https://doi.org/10.1007/s10858-004-4345-1
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DOI: https://doi.org/10.1007/s10858-004-4345-1