Biology Reference
In-Depth Information
poses a problem when attempting crystallization. Indeed, not many mem-
brane proteins are crystallized, and their structures are known. In this
chapter, we have presented a three-dimensional model of the P0 protein
with linked sugar moiety of the NHK-1 epitope. The model needs to be
tested experimentally; protein must therefore be purified and crystallized
before the three-dimensional arrangement of atoms can uncover its over-
all structure and shape. The P0 protein has one transmembrane spanning
segment, making the study of the protein very attractive.
For further calculations and analysis of the theoretical model of the P0
protein, predicted and estimated in this research, more work needs to be done
on molecular dynamics in the membrane and simulation of local energy min-
imization. The whole model of the glycoprotein also requires precise dock-
ing of the HNK-1 epitope and structural optimization of oligosaccharide.
Finally, deep database mining and clinical research are required to
establish whether the estimated autoimmune epitopes of the myelin P0
protein are able to be active autoimmune peptides in humans.
Acknowledgments
J.P. Jastrzebski is very grateful to Prof. Marcella Attimonelli (Bari, Italy)
for help in learning and understanding of bioinformatics, and for con-
structive criticism and support. He is also grateful to Katarzyna
Wi ´niewska and Izabela Dorocka for technical assistance and to his wife
Aneta Jastrze
bska for her encouragement.
References
Bjellqvist B, Hughes GJ, Pasquali Ch, Paquet N, Ravier F, Sanchez J-Ch,
Frutiger S, Hochstrasser DF. (1993) The focusing positions of
polypeptides in immobilized pH gradients can be predicted from their
amino acid sequences.
Electrophoresis
14
: 1023-1031.
Bond JB, Saavedra RA, Kirschner DA. (2001) Expression and purifica-
tion of the extracellular domain of human myelin Protein Zero.
Protein
Exp Purif
23
: 398-410.
Search WWH ::
Custom Search