Projects per year
Abstract
Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model.
Original language | English |
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Pages (from-to) | 139-153 |
Number of pages | 15 |
Journal | Methods (San Diego, Calif.) |
Volume | 70 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - Dec 2014 |
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Dive into the research topics of 'Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH'. Together they form a unique fingerprint.Projects
- 2 Finished
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Strategic Award: Wellcome Trust Technology Platform
Blow, J. (Investigator), Lamond, A. (Investigator) & Owen-Hughes, T. (Investigator)
1/01/13 → 30/09/18
Project: Research
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Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)
Owen-Hughes, T. (Investigator)
1/01/12 → 31/05/19
Project: Research
Profiles
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Owen-Hughes, Tom
- Molecular Cell and Developmental Biology - Professor of Chromatin Structure and Dynamics
Person: Academic