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András Perczel: [Publications] [Author Rank by year] [Co-authors] [Prefers] [Cites] [Cited by]

Publications of Author

  1. Zoltán Gáspári, Csaba P. Ortutay, András Perczel
    A simple fold with variations: the pacifastin inhibitor family. [Citation Graph (0, 0)][DBLP]
    Bioinformatics, 2004, v:20, n:4, pp:- [Journal]
  2. Tamás Beke, Imre G. Csizmadia, András Perczel
    On the flexibility of -peptides. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2004, v:25, n:2, pp:285-307 [Journal]
  3. Ilona Hudáky, Péter Hudáky, András Perczel
    Solvation model induced structural changes in peptides. A quantum chemical study on Ramachandran surfaces and conformers of alanine diamide using the polarizable continuum model. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2004, v:25, n:12, pp:1522-1531 [Journal]
  4. Péter Hudáky, Imre Jákli, Attila G. Császár, András Perczel
    Peptide models XXXI. Conformational properties of hydrophobic residues shaping the core of proteins. An ab initio study of N-formyl-L-valinamide and N-formyl-L-phenylalaninamide. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2001, v:22, n:7, pp:732-751 [Journal]
  5. Imre Jákli, András Perczel, Ödön Farkas, Attila G. Császár, Carlos P. Sosa, Imre G. Csizmadia
    Peptide models XXIII. Conformational model for polar side-chain containing amino acid residues: A comprehensive analysis of RHF, DFT, and MP2 properties of HCO-L-SER-NH2 . [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2000, v:21, n:8, pp:626-655 [Journal]
  6. 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. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2000, v:21, n:10, pp:882-900 [Journal]
  7. 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. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2003, v:24, n:10, pp:1157-1171 [Journal]
  8. András Perczel, Ödön Farkas, Imre G. Csizmadia
    Peptide models XVI. The identification of selected HCO - L - SER - NH2 conformers via a systematic grid search using ab initio potential energy surfaces. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 1996, v:17, n:7, pp:821-834 [Journal]
  9. András Perczel, Ödön Farkas, Imre Jákli, Igor A. Topol, Imre G. Csizmadia
    Peptide models. XXXIII. Extrapolation of low-level Hartree-Fock data of peptide conformation to large basis set SCF, MP2, DFT, and CCSD(T) results. The Ramachandran surface of alanine dipeptide computed at various levels of theory. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2003, v:24, n:9, pp:1026-1042 [Journal]
  10. András Perczel, Péter Hudáky, Anna K. Füzéry, Imre G. Csizmadia
    Stability issues of covalently and noncovalently bonded peptide subunits. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2004, v:25, n:8, pp:1084-1100 [Journal]
  11. 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. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2005, v:26, n:13, pp:1307-1317 [Journal]
  12. András Perczel, Zoltán Gáspári, Imre G. Csizmadia
    Structure and stability of -pleated sheets. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2005, v:26, n:11, pp:1155-1168 [Journal]
  13. Tamás Beke, Csaba Somlai, András Perczel
    Toward a rational design of -peptide structures. [Citation Graph (0, 0)][DBLP]
    Journal of Computational Chemistry, 2006, v:27, n:1, pp:20-38 [Journal]

  14. Fast protein fold estimation from NMR-derived distance restraints. [Citation Graph (, )][DBLP]


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