Bioinformatics of Myelin Membrane Proteins - Molecules: Nucleation, Aggregation and Crystallization - page 40

(Inouye, Kirschner, 1991 ), at a time when the term “bioinformatics” had
not even been invented (Boguski, 1998). It is interesting to compare the
results then and now.
Water Soluble Versus Integral Myelin Proteins
Myelin basic protein
Human MBP (Uniprot P02686) is 171 residues long. It is a water-soluble
protein that lacks both a signal peptide and putative transmembrane
helices (Fig. 1). Bovine myelin basic protein is the most studied protein;
it is remarkable for its “random coil” conformation in aqueous solutions,
Fig. 1. Analysis of human MBP by (a) the ∆ G app predictor and (b) SignalP 3.0. There is
no indication of transmembrane helices [i.e. segments with predicted ∆ G (Gibb's free
energy for membrane insertion) near or less than zero kcal/mol; note that negative values
are upwards. Sequence scans with different lengths are displayed in different colors]. The
SignalP predictor finds no indication of a signal peptide (i.e. there is no N-terminal
segment with n-, h- and c-region probabilities > 0.5).