1. Conformational Studies of an Undecapeptide Reproducing the Consensus Sequence Around the Cleavage Site of the RXVRG Endoprotease from Xenopus Laevis Skin Endoprotease.
D. Baron, A.- M. Leseney, F.- R. Chalaoux and J. Riand, Biopolymers, 34, 1419-1431 (1994).

2. NMR Conformational Study of a Model Tetradecapeptide Mimicking the RXVRG Consensus Cleavage Site of a Xenopus Laevis Skin Endoprotease.
F.- R. Chalaoux, J. Riand, A.- M. Leseney and D.Baron, Int. J. Pept. Prot. Res. , 45, 519 (1995).

3. Two Dimensional ¹H NMR Study of a Tetradecapeptide with the Consensus Sequence Arg⁵ - Asp - Val - Arg - Gly⁹ : Structural Effects of the Outside Substitution Ser¹² by Ala¹².
J. Riand, F.- R. Chalaoux, A.- M. Leseney and D. Baron, J. Biomol. Struct. Dynam. , 12, 993 (1995).

4. Conformational Study Based on Simulated Annealing and ¹H NMR of Peptides Comprissing the Consensus Sequence Arg⁵ - Asp - Val - Arg - Gly⁹ : Effects of the Substitution Ser¹² by Ala¹² or of 3 Residues Deletion at the N-Terminus.
S. Meddeb, D. Baron, J. Riand, J. P. Ballini, P. Vigny and J. Ph. Demaret, J. Biomol. Struct. Dynam. , 13, 661 (1996).

5. Solutions conformations of deltorphin-I obtained from combined use of quantitative 2D-NMR and energy calculations : a comparison with dermenkephalin.
Naïm, M. , Nicolas, P. , Benajiba, A. and Baron, D. , J. Peptide Res. , 52, 443-456 (1998).

6. The δ-selective Opioid Peptide Dermenkephalin and the μ-selective Hybrid Peptide Dermenkephalin - [1-4] - Dermorphin - [5-7] Display Strikingly Different Conformations Despite Identical Tetrapeptide N-Termini. A Quantitative 2-D NMR and Molecular Modeling Analysis.
Riand J. , Baron D. , Nicolas P. , Benajiba A. , Teng Y. and Naïm M. , J. Biomol. Struct. Dyn. , 17, 445-460 (1999).

7. The μ-selective Heptapeptide Opioid Dermorphin has Two Conformations Around Phe3 Φ with no Head-to-tail Interaction. A Quantitative 2-D NMR and Molecular Modeling Analysis.
Riand, J. , Nicolas, P. , and Baron, D. , J. Biomol. Struct. Dyn. , 20, 359-373 (2002).