The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …

Living organisms depend on timely and organized interactions between proteins linked in
interactomes of high complexity. The recent increased precision by which protein …

Abstract “Natively unfolded” proteins occupy a unique niche within the protein kingdom in
that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino …

The dominant view of protein structure-function is that an amino acid sequence specifies a
three-dimensional (3-D) structure that is a prerequisite for protein function. In contrast, many …

The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin
sheath in the central nervous system of higher vertebrates, and a member of a larger family …

The classic myelin basic protein (MBP) splice isoforms range in nominal molecular mass
from 14 to 21.5 kDa, and arise from the gene in the oligodendrocyte lineage (Golli) in …

The effect of deimination of arginyl residues in bovine myelin basic protein (MBP) on its
susceptibility to digestion by cathepsin D has been studied. Using bovine component 1 (C-1) …

Myelin basic protein (MBP) binds to negatively charged lipids on the cytosolic surface of
oligodendrocyte membranes and is responsible for adhesion of these surfaces in the …

The classic isoforms of myelin basic protein (MBP, 14–21.5 kDa) are essential to formation
of the multilamellar myelin sheath of the mammalian central nervous system (CNS). The …

Intrinsically disordered proteins lack a well-defined folded structure and contain a high
degree of structural freedom and conformational flexibility, which is expected to enhance …