Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
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Publication:5486442
DOI10.1088/0266-5611/22/4/019zbMATH Open1095.92033OpenAlexW2037965172WikidataQ58619106 ScholiaQ58619106MaRDI QIDQ5486442FDOQ5486442
Authors: Marco Longinetti, Claudio Luchinat, Giacomo Parigi, Luca Sgheri 
Publication date: 6 September 2006
Published in: Inverse Problems (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1088/0266-5611/22/4/019
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- Inferential structure determination from NMR data
- Restoring orientational distribution function of particles
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- Model-Based Assignment and Inference of Protein Backbone Nuclear Magnetic Resonances
- Extended Abstract: Structure Determination of Symmetric Protein Complexes by a Complete Search of Symmetry Configuration Space Using NMR Distance Restraints
- Looking for central tendencies in the conformational freedom of proteins using NMR measurements
- Conformational freedom of proteins and the maximal probability of sets of orientations
- Uniqueness and degeneracy in the localization of rigid structural elements in paramagnetic proteins
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