Chemical shift calculations of α-amino acids and peptides

Protein/peptide NMR structure determination could be speed up by using chemical shift information to establish backbone folding units. Especially, two- and three-dimensional NMR spectra can be useful in this respect. Our results suggest that such methods are viable because relevant correlations between backbone fold and 1Hα and 13Cα chemical shift values can be found. Our calculation methods comprise the GIAO-RHF formalism with the 6-31+G* and TZ2P basis sets. This indicates that the Ha, Ca, and Cb chemical shifts of alanine depend
considerably on the backbone fold of the parent residue also in proteins.

Csa3Csa2

Kapcsolódó publikációk

  • Péter Hudáky , András Perczel
    Toward direct determination of conformations of protein building units from multidimensional NMR experiments VI. Chemical shift analysis of His to gain 3D structure and protonation state information
    J. Comput. Chem. 26:1307-1317. (2005) Kivonat
  • András Czajlik , András Perczel
    Peptide Models XXXII. Computed chemical shift analysis of penetratin fragments
    J. Mol. Struct. (THEOCHEM) 675(1-3): 129-139. (2004) Kivonat
  • András Perczel , Anna K. Füzéry , Attila G. Császár
    Toward direct determination of conformations of protein building units from multidimensional NMR experiments. V. NMR chemical shielding analysis of N-formyl-serinamide, a model for polar side-chain containing peptides
    J. Comput. Chem. 24(10): 1157-1171. (2003) Kivonat
  • Eszter Czinki , Attila G. Császár , András Perczel
    A theoretical case study of type I and type II β-turns
    Chem Eur J 9(5): 1182-1191 (2003) Kivonat
  • András Perczel , Attila G. Császár
    Toward direct determination of conformations of protein building units from multidimensional NMR experiments III-A theoretical case study of For-L-Phe-NH2.
    Eur. Phys. J. D20: 513-530. (2002)
  • András Perczel , Attila G. Császár
    Toward direct determination of conformations of protein building units from multidimensional NMR experiments part II: A theoretical case study of formyl-L-valine amide.
    Chem Eur J 7: 1069-1083. (2001) Kivonat
  • András Perczel , Attila G. Császár
    Toward direct determination of conformations of protein building units from multidimensional NMR experiments I. A theoretical case study of For-Gly-NH2 and For-L-Ala-NH2.
    J. Comput. Chem. 21: 882-900. (2000) Kivonat
  • András Czajlik , Ilona Hudáky , András Perczel
    Local Protein Backbone Folds Determined by Calculated NMR Chemical Shifts
    JOURNAL OF COMPUTATIONAL CHEMISTRY 32:(16) pp. 3362-3382. (2011)