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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., , , and . J. Comput. Chem., 22 (7): 732-751 (2001)Fast protein fold estimation from NMR-derived distance restraints., , , and . Bioinform., 24 (2): 272-275 (2008)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., and . J. Comput. Chem., 21 (10): 882-900 (2000)Four faces of the interaction between ions and aromatic rings., , , , and . Journal of Computational Chemistry, 38 (20): 1762-1773 (2017)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 ., , , , , and . J. Comput. Chem., 21 (8): 626-655 (2000)Opening Amyloid-Windows to the secondary structure of proteins: The amyloidogenecity increases tenfold inside beta-sheets., , , , and . Comput. Biol. Medicine, (2024)Combined NMR three-bond scalar coupling measurements and QM calculations to calculate OH-rotamer equilibrium of polyalcohols., , , and . J. Comput. Chem., 30 (4): 540-550 (2009)On the flexibility of -peptides., , and . J. Comput. Chem., 25 (2): 285-307 (2004)Omicron Binding Mode: Contact Analysis and Dynamics of the Omicron Receptor-Binding Domain in Complex with ACE2., , and . J. Chem. Inf. Model., 62 (16): 3844-3853 (2022)