A new model for chemical shifts of amide hydrogens in proteins
- 260 Downloads
We propose a new computational model to predict amide proton chemical shifts in proteins. In addition to the ring-current, susceptibility and electrostatic effects of earlier models, we add a hydrogen-bonding term based on density functional calculations of model peptide–peptide and peptide–water systems. Both distance and angular terms are included, and the results are rationalized in terms of natural bond orbital analysis of the interactions. Comparison to observed shifts for 15 proteins shows a significant improvement over existing structure-shift correlations. These additions are incorporated in a new version of the SHIFTS program.
KeywordsChemical shifts Proteins Amide hydrogen
This work was supported by NIH grant GM45811. We thank Jan Ziegler, Stephan Schwarzinger and Jan Jensen for helpful discussions.
- Frisch MJ, Trucks GW, Schlegel HB, Gill PMW, Johnson BG, Robb JA, Cheeseman JR, Keith TA, Petersson GA, Montgomery JA, Raghavachari K, Al-Laham MA, Zakrzewski VG, Ortiz JV, Foresman JB, Cioslowski J, Stefanov BB, Nanayakkara A, Challacombe M, Peng CY, Ayala PY, Chen W, Wong MW, Andres JL, Replogle ES, Gomperts R, Martin RL, Fox DJ, Binkley JS, Defrees DJ, Baker J, Stewart JP, Head-Gordon M, Gonzalez C, Pople JA (1998) Gaussian 98 (Revision A9). Gaussian Inc, Pittsburgh PAGoogle Scholar
- Perdew JP, Wang Y (1992) Accurate and simple analytic representation of the electron-gas correlation energy. Phys Rev B 45:13244–13249Google Scholar
- Rumelhart DE, McClelland J (1986) Parallel distrbuted processing. MIT Press, BostonGoogle Scholar
- Zupan J, Gasteiger J (1993) Neural networks for chemists. VCH Verlagsgesellschaft mbH, WeinheimGoogle Scholar