Measurement of four-bond HN-H alpha J-couplings in staphylococcal nuclease.
Quantitative J-correlation and triple-resonance ECOSY-type experiments are used to unambiguously establish the presence of four-bond sequential HN-H alpha J-couplings in the protein staphylococcal nuclease. Substantially negative 4JH alpha HN values, ranging from -0.8 to -2.3 Hz, are observed when the psi angle is near +120 degrees, and the following phi angle near +60 degrees. For other conformations, the four-bond HN-H alpha J-couplings fall between -0.5 and +0.5 Hz.
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
G W
GW
Vuister
A
A
Bax
D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008836:Micrococcal Nuclease / Q000737:chemistry*; D011487:Protein Conformation
D008836:Micrococcal Nuclease