Bioinformatics

The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.

Vranken, W. F., Budesinsky M., Fant F., Boulez K., and Borremans F. A., "The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.", FEBS Lett, vol. 374, issue 1, pp. 117-21, 1995 Oct 23.

Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.

Vranken, W. F., Budesinsky M., Martins J. C., Fant F., Boulez K., Gras-Masse H., and Borremans F. A., "Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.", Eur J Biochem, vol. 236, issue 1, pp. 100-8, 1996 Feb 15.

A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein.

Vranken, W. F., Chen Z. G., Xu P., James S., Bennett H. P., and Ni F., "A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein.", J Pept Res, vol. 53, issue 5, pp. 590-7, 1999 May.

The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.

Fant, F., Vranken W. F., and Borremans F. A., "The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.", Proteins, vol. 37, issue 3, pp. 388-403, 1999 Nov 15.

Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution.

Vranken, W. F., Fant F., Budesinsky M., and Borremans F. A., "Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution.", Eur J Biochem, vol. 268, issue 9, pp. 2620-8, 2001 May.

Solution structures of a 30-residue amino-terminal domain of the carp granulin-1 protein and its amino-terminally truncated 3-30 subfragment: implications for the conformational stability of the stack of two beta-hairpins.

Vranken, W. F., James S., Bennett H. P. J., and Ni F., "Solution structures of a 30-residue amino-terminal domain of the carp granulin-1 protein and its amino-terminally truncated 3-30 subfragment: implications for the conformational stability of the stack of two beta-hairpins.", Proteins, vol. 47, issue 1, pp. 14-24, 2002 Apr 1.

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