NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein.
We report the NMR assignment of 18.5 kDa recombinant murine myelin basic protein (MBP) in 100 mM KCl as a prerequisite to structural analyses of its Ca2+-dependent interaction with calmodulin.
Libich
David S
DS
Department of Molecular and Cellular Biology, Biophysics Interdepartmental Group, University of Guelph, Guelph, ON, Canada.
Monette
Martine M
MM
Robertson
Valerie J
VJ
Harauz
George
G
D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D051379:Mice; D015394:Molecular Structure; D008970:Molecular Weight; D004676:Myelin Basic Protein; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D002147:Calmodulin; C499047:Mbp protein, mouse; D004676:Myelin Basic Protein; D009419:Nerve Tissue Proteins; D020033:Protein Isoforms; D011994:Recombinant Proteins; D014157:Transcription Factors