Bioinformatics of Myelin Membrane Proteins - Molecules: Nucleation, Aggregation and Crystallization - page 35

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Bioinformatics of Myelin
Membrane Proteins

Gunnar von Heijne* ,† and Jan Sedzik ‡

While tertiary structure cannot in general be predicted for membrane proteins,
membrane topology is easier to predict. In this chapter, our focus is on the proteins
found in the myelin membrane. The myelin membrane is unique, since it contains
almost 80% (w/w) lipids, making it one of the most lipid-rich biomembranes. Not
all abundant myelin proteins are membrane proteins; there are also water soluble
proteins. The difference between these two types of proteins can easily be detected
by studying the amino acid sequence of the proteins. In this chapter, we present pre-
dictions of the membrane topology and the presence/absence of signal peptides in
the myelin proteins, and discuss the results in light of published experimental data.

Keywords: Crystallogenesis; bioinformatics; membrane; protein; lipid; myelin

sheath.

Introduction

The rapid development of bioinformatics in recent years has been driven
to a large extent by the accumulation of large databases, compiling
amino acid sequences of proteins and sequences of nucleotides in nucleic
acids. Obviously, to extract biologically relevant information from such

*Corresponding author.
† Gunnar von Heijne, Department of Biochemistry and Biophysics, Stockholm University,
SE-10691 Stockholm, Sweden. Email: [e-mail].
‡ Protein Crystallization Facility, Department of Neurobiology, Care Sciences and Society,
NOVUM, Karolinska Institutet, Stockholm, Sweden, and Department of Chemical
Engineering and Technology, Protein Crystallization Facility, KTH, Teknikringen 28,
100 44 Stockholm, Sweden. E-mail: [e-mail].