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Journal of Molecular Biology|April 5, 1992
Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filteringG Esposito, A M Lesk, H Molinari, et al.Biopolymers|May 1, 1993
Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteinsG Esposito, A M Lesk, H Molinari, et al.Journal of Molecular Biology|November 2, 1999
Unfolding and refolding of bovine beta-lactoglobulin monitored by hydrogen exchange measurementsL Ragona, F Fogolari, S Romagnoli, et al.Biochimica Et Biophysica Acta|February 13, 1992
H-NMR studies of native and fragmented subtilisin CarlsbergR Consonni, H Molinari, F Greco, et al.Proteins|May 17, 2000
Electrostatic properties of bovine beta-lactoglobulinF Fogolari, L Ragona, S Licciardi, et al.FEBS Letters|September 25, 1995
1H-NMR and photo-CIDNP spectroscopies show a possible role for Trp23 and Phe31 in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricusR Consonni, R Limiroli, H Molinari, et al.FEBS Letters|October 22, 1998
Monomeric bovine beta-lactoglobulin adopts a beta-barrel fold at pH 2F Fogolari, L Ragona, L Zetta, et al.Journal of Peptide Science : an Official Publication of the European Peptide Society|December 10, 1997
The design of a specific ligand of HIV gp120M Scarselli, A Facchiano, G Russo, et al.FEBS Letters|March 4, 1996
Partially folded structure of monomeric bovine beta-lactoglobulinH Molinari, L Ragona, L Varani, et al.Pageof 9