Anomalous amide proton chemical shifts as signatures of hydrogen bonding to aromatic sidechains
Kumaran Baskaran,Colin W. Wilburn,Jonathan R. Wedell,Leonardus M. I. Koharudin,Eldon L. Ulrich,Adam D. Schuyler,Hamid R. Eghbalnia,Angela M. Gronenborn,and Jeffrey C. Hoch
Kumaran Baskaran
Department of Molecular Biology and Biophysics, UConn Health, 263
Farmington Ave., Farmington, CT 06030-3305 USA
Colin W. Wilburn
Department of Molecular Biology and Biophysics, UConn Health, 263
Farmington Ave., Farmington, CT 06030-3305 USA
Jonathan R. Wedell
Department of Molecular Biology and Biophysics, UConn Health, 263
Farmington Ave., Farmington, CT 06030-3305 USA
Leonardus M. I. Koharudin
Department of Structural Biology University of Pittsburgh School of
Medicine 3501 Fifth Ave., Pittsburgh, PA 15260 USA
Eldon L. Ulrich
Department of Molecular Biology and Biophysics, UConn Health, 263
Farmington Ave., Farmington, CT 06030-3305 USA
The Biological Magnetic Resonance Data Bank (BMRB) has been used to identify overall trends, for example, the relationship between chemical shift and backbone conformation. The BMRB archive has grown so that statistical outliers are sufficiently numerous to afford insights into unusual or unique structural features in proteins. We analyze amide proton chemical shift outliers to gain insights into the occurrence of hydrogen bonds between an amide NH and the p-pi cloud of aromatic sidechains.
The Biological Magnetic Resonance Data Bank (BMRB) has been used to identify overall trends, for...