Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage

• Published in: Journal of biomolecular NMR Vol. 20; no. 4; pp. 365 - 377
• Main Authors: Zweckstetter, M, Bax, A
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01-08-2001
• Subjects: Antigens, Bacterial - chemistry; Antigens, Bacterial - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacteriophage Pf1 - chemistry; Bacteriophage Pf1 - metabolism; Carbon Radioisotopes - chemistry; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Humans; Magnetic fields; Magnetism; Nitrogen Radioisotopes - chemistry; Nuclear Magnetic Resonance, Biomolecular; Osmolar Concentration; Protons; Sodium chloride; Solutions; Studies; Temperature; Ubiquitin - chemistry; Ubiquitin - metabolism; Water - chemistry
• ISSN: 0925-2738; 1573-5001
• DOI: 10.1023/a:1011263920003

The phase diagram of Pf1 solutions has been studied indirectly by observation of 2H quadrupole splittings of the solvent signal and measurement of dipolar couplings in solute macromolecules. At low volume fractions of Pf1 and at high ionic strength, alignment of both the phage and the solute depends strongly on the strength of the magnetic field. Both the theoretical and experimentally determined phase diagram of Pf1 show that at low concentrations and high ionic strengths the solution becomes isotropic. However, just below the nematic phase boundary the behavior of the system is paranematic, with cooperative alignment which depends on the strength of the applied magnetic field. Above 16 mg/ml Pf1 is fully nematic up to 600 mM NaCl. Alignment of proteins with a significant electric dipole moment, which tends to be strong in Pf1, can be reduced by either high ionic strength or low phage concentration. Because ionic strength modulates both the orientation and magnitude of the alignment tensor in Pf1 medium, measurement at two ionic strengths can yield linearly independent alignment tensors.