Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.
The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported. The splittings appear as small field-dependent perturbations of normal scalar couplings. Assignment of more than 90 resonances to specific sequential sites in the protein allows correlation of the dipolar contributions with predictions based on the known susceptibility and known structure of the protein. Implications as an additional source of information for protein structure determination in solution are discussed.
Tolman
J R
JR
Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
Flanagan
J M
JM
Kennedy
M A
MA
Prestegard
J H
JH
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli; D006418:Heme / Q000032:analysis; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008786:Metmyoglobin / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D012984:Software; D012996:Solutions
D009211:Myoglobin; D009587:Nitrogen Isotopes; D011506:Proteins; D011994:Recombinant Proteins; D012996:Solutions; C007177:cyanometmyoglobin; D008786:Metmyoglobin; D006418:Heme; D006859:Hydrogen