Magnetic susceptibility-induced alignment of proteins in reverse micelles.
Proteins encapsulated within the aqueous core of reverse micelles are found to partially align in a magnetic field. The degree of alignment is sufficient to result in sizable residual 15N-1H dipolar couplings that can be easily measured. It is found that the magnetic susceptibility of the reverse micelle particle is not dominated by the encapsulated protein. The residual dipolar couplings are found to be structurally meaningful.
Valentine
Kathleen G
KG
Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA.
Pometun
Maxim S
MS
Kielec
Joseph M
JM
Baigelman
Robert E
RE
Staub
Jayme K
JK
Owens
Kristy L
KL
Wand
A Joshua
AJ
D008280:Magnetics; D008823:Micelles; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D008823:Micelles; D011506:Proteins