Thermodynamic analysis of the disorder-to-α-helical transition of 18.5-kDa myelin basic protein reveals an equilibrium intermediate representing the most compact …

KA Vassall, AD Jenkins, VV Bamm, G Harauz - Journal of molecular biology, 2015 - Elsevier
Abstract The intrinsically disordered, 18.5-kDa isoform of myelin basic protein (MBP) is a
peripheral membrane protein that is essential to proper myelin formation in the central …

[HTML][HTML] Substitutions mimicking deimination and phosphorylation of 18.5-kDa myelin basic protein exert local structural effects that subtly influence its global folding

KA Vassall, VV Bamm, AD Jenkins, CJ Velte… - … et Biophysica Acta (BBA …, 2016 - Elsevier
Intrinsically-disordered proteins (IDPs) present a complex interplay of conformational
variability and multifunctionality, modulated by environment and post-translational …

[HTML][HTML] The intrinsically disordered protein glue of the myelin major dense line: Linking AlphaFold2 predictions to experimental data

OC Krokengen, A Raasakka, P Kursula - Biochemistry and biophysics …, 2023 - Elsevier
Numerous human proteins are classified as intrinsically disordered proteins (IDPs). Due to
their physicochemical properties, high-resolution structural information about IDPs is …

The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein

KA Vassall, K Bessonov, M De Avila, E Polverini… - PloS one, 2013 - journals.plos.org
The classic isoforms of myelin basic protein (MBP) are essential for the formation and
maintenance of myelin in the central nervous system of higher vertebrates. The protein is …

Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein

CM Hill, IR Bates, GF White, FR Hallett… - Journal of structural …, 2002 - Elsevier
The osmolyte trimethylamine-N-oxide (TMAO) is a naturally in vivo occurring “chemical
chaperone” that has been shown to stabilise the folding of numerous proteins. Myelin basic …

[HTML][HTML] Conformational choreography of a molecular switch region in myelin basic protein—Molecular dynamics shows induced folding and secondary structure type …

E Polverini, EP Coll, DP Tieleman, G Harauz - Biochimica et Biophysica …, 2011 - Elsevier
The 18.5 kDa isoform of myelin basic protein is essential to maintaining the close apposition
of myelin membranes in central nervous system myelin, but its intrinsic disorder …

Solution NMR structure of an immunodominant epitope of myelin basic protein: conformational dependence on environment of an intrinsically unstructured protein

C Farès, DS Libich, G Harauz - The FEBS journal, 2006 - Wiley Online Library
Using solution NMR spectroscopy, three‐dimensional structures have been obtained for an
18‐residue synthetic polypeptide fragment of 18.5 kDa myelin basic protein (MBP, human …

Divalent cations induce a compaction of intrinsically disordered myelin basic protein

C Baran, GST Smith, VV Bamm, G Harauz… - … and biophysical research …, 2010 - Elsevier
Central nervous system myelin is a dynamic entity arising from membrane processes
extended from oligodendrocytes, which form a tightly-wrapped multilamellar structure …

Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic …

MAM Ahmed, VV Bamm, L Shi, M Steiner-Mosonyi… - Biophysical …, 2009 - cell.com
The 18.5 kDa isoform of myelin basic protein (MBP) is a peripheral membrane protein that
maintains the structural integrity of the myelin sheath of the central nervous system by …

Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient α-helices and a calmodulin-binding site

DS Libich, G Harauz - Biophysical journal, 2008 - cell.com
The 18.5 kDa isoform of myelin basic protein (MBP) is the predominant form in adult human
central nervous system myelin. It is an intrinsically disordered protein that functions both in …