Conformational analysis of t immunogenic peptides by circular dichroism spectroscopy
Chantal Abergel
Laboratoire de Cristallogénèse et de Cristallographie des Macromolécules Biologiques URA 232-CNRS
Search for more papers by this authorCorresponding Author
Jean-Michel Claverie
Unité Informatique Scientifique, Institut Pasteur, Paris
Unité Informatique Scientifique, Institut Pasteur, 28, rue du Dr. Roux, F-75724 Paris Cedex 15, FranceSearch for more papers by this authorChantal Abergel
Laboratoire de Cristallogénèse et de Cristallographie des Macromolécules Biologiques URA 232-CNRS
Search for more papers by this authorCorresponding Author
Jean-Michel Claverie
Unité Informatique Scientifique, Institut Pasteur, Paris
Unité Informatique Scientifique, Institut Pasteur, 28, rue du Dr. Roux, F-75724 Paris Cedex 15, FranceSearch for more papers by this authorAbstract
The structure of two T-immunogenic peptides, one from the gag p24 protein of the human immunodeficiency virus, the other from the 11.1 gene product of Plasmodium falciparum, was studied by circular dichroism spectroscopy in various pH and solvent conditions. Although both sequences are predicted to adopt an alpha-helical conformation and one of them is a repeat of a perfect alpha-amphipathic sequence pattern, these two peptides exhibit a strong propensity to adopt an extended, turn or aperiodical conformation in solution.
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