scholarly journals Interaction of the 18.5-kD isoform of myelin basic protein with Ca2+-calmodulin: Effects of deimination assessed by intrinsic Trp fluorescence spectroscopy, dynamic light scattering, and circular dichroism

2003 ◽  
Vol 12 (7) ◽  
pp. 1507-1521 ◽  
Author(s):  
David S. Libich ◽  
Christopher M.D. Hill ◽  
Ian R. Bates ◽  
F. Ross Hallett ◽  
Souzan Armstrong ◽  
...  
SURG Journal ◽  
2014 ◽  
Vol 7 (3) ◽  
pp. 30-41
Author(s):  
Danielle K. Lanthier ◽  
Kenrick A. Vassall ◽  
George Harauz

Myelin Basic Protein (MBP) is a highly abundant protein in central nervous system (CNS) myelin that has a critical role in its proper formation and functioning. The 21.5-kDa isoform of MBP has been shown to be selectively imported into the nucleus of myelin-producing cells, oligodendrocytes, and may be involved in signaling pathways that affect the formation and recovery of CNS myelin. The first step in understanding potential nuclear binding partners of 21.5-kDa MBP is to characterize the structure of the protein. In this study, circular dichroism and fluorescence spectroscopy were used to analyze the structure of 21.5-kDa rmMBP (recombinant murine MBP) in vitro in the presence and absence of Zn2+, an abundant trace metal in CNS myelin that has been suggested to affect MBP structure. Fluorescence spectroscopy with a probe for hydrophobic protein regions showed that Zn2+ may affect the conformation of 21.5-kDa MBP in aqueous solution. Keywords: myelin basic protein (MBP); intrinsically-disordered protein; circular dichroism; fluoresence spectroscopy


2009 ◽  
Vol 113 (51) ◽  
pp. 16420-16424 ◽  
Author(s):  
Alessandro Esposito ◽  
Lucia Comez ◽  
Stefania Cinelli ◽  
Filippo Scarponi ◽  
Giuseppe Onori

PLoS ONE ◽  
2020 ◽  
Vol 15 (4) ◽  
pp. e0221180
Author(s):  
Yuejiao Xian ◽  
Brenda Moreno ◽  
Victoria Miranda ◽  
Neha Vijay ◽  
Luis C. Nunez ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document