Evidence of molecular alignment fluctuations in aqueous dilute liquid crystalline media.
Protein dynamics can be studied by NMR measurements of aqueous dilute liquid crystalline samples. However, the measured residual dipolar couplings are sensitive not only to internal fluctuations but to all changes in internuclear vectors relative to the laboratory frame. We show that side-chain fluctuations and bond librations in the ps-ns time scale perturb the molecular shape and charge distribution of a small globular protein sufficiently to cause a noticeable variation in the molecular alignment. The alignment variation disperses the bond vectors of a conformational ensemble even further from the dispersion already caused by internal fluctuations of a protein. Consequently RDC-probed order parameters are lower than those obtained by laboratory frame relaxation measurements.
Louhivuori
Martti
M
Department of Physical Sciences, University of Helsinki, Gustaf Hällströmin katu 2, Helsinki 00014, Finland. m.j.louhivuori@rug.nl
Otten
Renee
R
Salminen
Tapio
T
Annila
Arto
A
D002135:Calcium-Binding Proteins / Q000737:chemistry; D003198:Computer Simulation; D003460:Crystallization; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry
D002135:Calcium-Binding Proteins; D025801:Ubiquitin
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