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NMR signal assignments of amide protons in the. cap alpha. -helical domains of staphylococcal nuclease

Journal Article · · Biochemistry; (United States)
OSTI ID:6901490

The authors report complete assignments of the amide proton signals in the three long d/sub NN/ connectivity sequences observed in the NOESY spectrum of deuteriated staphylococcal nuclease (Nase) complexed with thymidine 3',5'-bisphosphate (pdTp) and Ca/sup 2 +/, M/sub r/ 18K. The assignments are made by comparing NOESY spectra with /sup 1/H-/sup 15/N and /sup 1/H-/sup 13/C heteronuclear multiple-quantum shift correlation (HMQC) spectra of Nase samples containing /sup 15/N- and /sup 13/C-labeled amino acids. The assignments show that the residues which are linked by the d/sub NN/ connectivity sequences are located in the three ..cap alpha..-helical domains of Nase. The results indicate that by combining NOESY and HMQC spectra of appropriately labeled samples it should be possible to delineate and study ..cap alpha..-helical domains in soluble proteins having molecular weights that are greater than 18K.

Research Organization:
National Institutes of Health, Bethesda, MD (USA)
OSTI ID:
6901490
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:14; ISSN BICHA
Country of Publication:
United States
Language:
English