ArticleJournal of biomolecular NMR2004
Alignment of chain-like molecules.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Computational Studies of Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2018Article
- Ensemble-based interpretations of NMR structural data to describe protein internal dynamics.Molecules (Basel, Switzerland) · 2013Review
- Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.Journal of biomolecular NMR · 2009Article
- Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP.Journal of biomolecular NMR · 2008Article
- The effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in Tau.PLoS computational biology · 2008Article
- Theoretical framework for NMR residual dipolar couplings in unfolded proteins.Journal of biomolecular NMR · 2007Article
- A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A set of HA-detected experiments for measuring scalar and residual dipolar couplings.Journal of biomolecular NMR · 2005Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The steric obstruction model, that describes the enhanced alignment of folded proteins by anisotropic medium, is extended to account for the residual dipolar couplings of chain-like polypeptides. The average alignment of each chain segment is calculated from an ensemble of conformations represented by a spatial probability distribution. The segmental alignment depends on chain length, flexibility and segment's position in the chain. Residual dipolar couplings in turn depend on internuclear vector directions within each fragment. The results of calculations and simulations explain salient features of the experimental data. With this insight residual dipolar couplings can be interpreted to assess the degree of denaturation, local structures and spatial organization of weakly structured proteins.
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Registered trials
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