Protein docking using an ensemble of spin labels optimized by intra-molecular paramagnetic relaxation enhancement

Author:

Schilder Jesika12345,Liu Wei-Min12345,Kumar Pravin67285,Overhand Mark12345,Huber Martina67285,Ubbink Marcellus12345

Affiliation:

1. Leiden Institute of Chemistry

2. Leiden University

3. Gorlaeus Laboratories

4. 2333 CC Leiden

5. The Netherlands

6. Department of Physics

7. Huygens-Kamerlingh Onnes Laboratory

8. 2333 CA Leiden

Abstract

The effect of spin label mobility on the accuracy of protein–protein docking calculations was investigated using inter- and intra-molecular PRE data.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference51 articles.

1. Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation

2. J. Schilder , M. A. S.Hass, P. H.Keizers and M.Ubbink, Paramagnetic NMR spectroscopy and lowly populated states, in Recent Developments in Biomolecular NMR, ed. M. G. Clore and J. Potts, Royal Society of Chemistry, 2012, pp. 130–150

3. A NITROXIDE-MALEIMIDE SPIN LABEL

4. Chapter 2 The hyperfine shift

5. Utilization of Site-Directed Spin Labeling and High-Resolution Heteronuclear Nuclear Magnetic Resonance for Global Fold Determination of Large Proteins with Limited Nuclear Overhauser Effect Data

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