Looking for central tendencies in the conformational freedom of proteins using NMR measurements
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Publication:2965693
DOI10.1088/1361-6420/AA54EAzbMATH Open1394.92096arXiv1602.05953OpenAlexW2276868786MaRDI QIDQ2965693FDOQ2965693
Authors: Luca Sgheri, Fabrizio Clarelli 
Publication date: 3 March 2017
Published in: Inverse Problems (Search for Journal in Brave)
Abstract: We study the conformational freedom of a protein made by two rigid domains connected by a flexible linker. The conformational freedom is represented as an unknown probability distribution on the space of allowed states. A new algorithm for the calculation of the Maximum Allowable Probability is proposed, which can be extended to any type of measurements. In this paper we use Pseudo Contact Shifts and Residual Dipolar Coupling. We reconstruct a single central tendency in the distribution and discuss in depth the results.
Full work available at URL: https://arxiv.org/abs/1602.05953
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Applications of statistics to biology and medical sciences; meta analysis (62P10) Protein sequences, DNA sequences (92D20)
Cites Work
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- Reconstruction of orientations of a moving protein domain from paramagnetic data
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Cited In (5)
- Joining RDC data from flexible protein domains
- Reconstruction of orientations of a moving protein domain from paramagnetic data
- Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
- Sampling of conformation space in torsion angle dynamics calculations
- Conformational freedom of proteins and the maximal probability of sets of orientations
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