Myoglobin solid-state study

Susi et al. (1967) have observed spectra of poly-L-lysine, poly-L-glutamic acid, )S-lactoglobulin, myoglobin, and a -casein in the region of absorption of the amide I band in HjO and DjO solutions, and in the solid state. Their results indicated that characteristic frequencies exhibited by specific conformations of the synthetic polypeptides studied are not transferable to corresponding conformations of globular proteins. 

Proteins consist essentially of one or more large polypeptides chains. The first solid-state NMR spectra of proteins were reported in 1991 by Oldfield and co-workers [13], which successfully acquired static powder spectra of a 67 kDa tetramer [ O2]haemoglobin and a 17 kDa [ 02]myo-globin sample. In 1998, the same team [13] recorded MAS NMR spectra of [ 02] myoglobin at 11.7 T, from which a Cq of less than 2 MHz was derived. Unfortunately, no further studies were published until 2010, thanks to the advanced NMR instrumentation and methodology, Wu and co-workers [37] reported a MAS NMR study at 21.14 T of two protein-ligand complexes, the egg-white avidin-[ 02]biotin (64 kDa) and... 

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