Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low protein concentrations (<or=100 microM) and at two field strengths (14.4 and 18.8 T) for 135 of 162 backbone amide groups. Rotational diffusion of the OMP was found to be axially symmetric with D( parallel)/D( perpendicular) = 1.20 +/- 0.02 with an overall global correlation time of 8.93 +/- 0.03 ns. Model-free internal dynamic analyses of these data provided a description of the protein's dynamics on multiple time scales. The results of these studies indicate that there is a large degree of conformational flexibility for alpha-helix 1 (alpha1), loop 1, and the conserved Omega-loop (loop 3). The functional significance that these dynamic regions of OMP have in modulating olfactory signal transduction is discussed.
Gitti
Rossitza K
RK
Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, Maryland 21201, USA.
Wright
Nathan T
NT
Margolis
Joyce W
JW
Varney
Kristen M
KM
Weber
David J
DJ
Margolis
Frank L
FL
D000818:Animals; D016880:Anisotropy; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000502:physiology; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D051842:Olfactory Marker Protein; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051381:Rats; D015398:Signal Transduction / Q000502:physiology; D012996:Solutions; D013816:Thermodynamics
D009419:Nerve Tissue Proteins; D009587:Nitrogen Isotopes; D051842:Olfactory Marker Protein; C497599:Omp protein, rat; D012996:Solutions