| Omicron Binding Mode: Contact Analysis and Dynamics of the Omicron Receptor-Binding Domain in Complex with ACE2. | 0 | 0.34 | 2022 |
| Four faces of the interaction between ions and aromatic rings. | 0 | 0.34 | 2017 |
| Predictable Conformational Diversity in Foldamers of Sugar Amino Acids. | 0 | 0.34 | 2017 |
| Local protein backbone folds determined by calculated NMR chemical shifts. | 0 | 0.34 | 2011 |
| Stability of the hydration layer of tropocollagen: A QM study. | 0 | 0.34 | 2010 |
| Combined NMR three-bond scalar coupling measurements and QM calculations to calculate OH-rotamer equilibrium of polyalcohols. | 0 | 0.34 | 2009 |
| How stable is a collagen triple helix? An ab initio study on various collagen and beta-sheet forming sequences | 1 | 0.48 | 2008 |
| Fast protein fold estimation from NMR-derived distance restraints | 1 | 0.40 | 2008 |
| Toward a rational design of -peptide structures | 0 | 0.34 | 2006 |
| Structure and stability of -pleated sheets | 3 | 1.40 | 2005 |
| 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. | 0 | 0.34 | 2005 |
| Stability issues of covalently and noncovalently bonded peptide subunits. | 1 | 0.40 | 2004 |
| Solvation model induced structural changes in peptides. A quantum chemical study on Ramachandran surfaces and conformers of alanine diamide using the polarizable continuum model. | 4 | 0.57 | 2004 |
| On the flexibility of -peptides | 0 | 0.34 | 2004 |
| A simple fold with variations: the pacifastin inhibitor family. | 1 | 0.78 | 2004 |
| 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. | 10 | 1.80 | 2003 |
| 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. | 2 | 0.49 | 2003 |
| 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 | 4 | 0.82 | 2001 |
| 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 | 3 | 1.27 | 2000 |
| 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 | 7 | 2.86 | 2000 |
| Peptide models XVI. The identification of selected HCO - L - SER - NH2 conformers via a systematic grid search using ab initio potential energy surfaces | 2 | 2.32 | 1996 |
