ArticleJournal of biomolecular NMR2007
Evidence of molecular alignment fluctuations in aqueous dilute liquid crystalline media.
Article in Journal of biomolecular NMR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.Biophysical reviews · 2012Review
- CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.BMC structural biology · 2010Article
- Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Journal of biomolecular NMR · 2008Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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Abstract
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.
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