Protein Structure Determination by Assembling Super-Secondary Structure Motifs Using Pseudocontact Shifts
نویسندگان
چکیده
منابع مشابه
Protein Structure Determination by Assembling Super-Secondary Structure Motifs Using Pseudocontact Shifts.
Computational and nuclear magnetic resonance hybrid approaches provide efficient tools for 3D structure determination of small proteins, but currently available algorithms struggle to perform with larger proteins. Here we demonstrate a new computational algorithm that assembles the 3D structure of a protein from its constituent super-secondary structural motifs (Smotifs) with the help of pseudo...
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Paramagnetic metal ions generate pseudocontact shifts (PCSs) in nuclear magnetic resonance spectra that are manifested as easily measurable changes in chemical shifts. Metals can be incorporated into proteins through metal binding tags, and PCS data constitute powerful long-range restraints on the positions of nuclear spins relative to the coordinate system of the magnetic susceptibility anisot...
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Obtaining enough experimental restraints can be a limiting factor in the NMR structure determination of larger proteins. This is particularly the case for large assemblies such as membrane proteins that have been solubilized in a membrane-mimicking environment. Whilst in such cases extensive deuteration strategies are regularly utilised with the aim to improve the spectral quality, these scheme...
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Acknowledgements This thesis represents the work I have carried out as a PhD student under the supervision of Professor Jan H. Jensen in his group of Biocomputational Chemistry. Thank you to all who have supported me during my work at the third floor of C-building at the H.C. Ørsteds Institute. I would especially like to thank the following people: • Thank you to my supervisor, Jan " Yoda " Jen...
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In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal ε domain of the E. coli DNA polymerase III (ε186) in complex...
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ژورنال
عنوان ژورنال: Structure
سال: 2017
ISSN: 0969-2126
DOI: 10.1016/j.str.2017.01.011