Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase.
Two-dimensional nuclear magnetic resonance spectroscopy has been used to study the bacterial ribonuclease barnase (MW 12,382). Resonance assignments have been made for protons in all of the 110 residues. Analysis of medium- and long-range contacts in NOESY spectra has demonstrated that the major elements of secondary structure in barnase in solution are essentially identical with those found in the crystal structure.
Bycroft
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MRC Unit for Protein Function and Design, University Chemical Laboratory, Cambridge, U.K.
Sheppard
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Lau
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Fersht
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004926:Escherichia coli / Q000201:enzymology*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012260:Ribonucleases / Q000302:isolation & purification; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D006859:Hydrogen; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease