ArticleJournal of the American Chemical Society2009
Selective characterization of microsecond motions in proteins by NMR relaxation.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- An optimizedJournal of biomolecular NMR · 2025Article
- Extending the detectable time window of fast protein dynamics usingJournal of biomolecular NMR · 2025Article
- Structural and Functional Relevance of Charge Based Transient Interactions inside Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
- Correlating histone acetylation with nucleosome core particle dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Protein Dynamics revealed by NMR Relaxation Methods.Emerging topics in life sciences · 2020Article
- Detection of chemical exchange in methyl groups of macromolecules.Journal of biomolecular NMR · 2019Article
- Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance RChemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019Review
- Why the Energy Landscape of Barnase Is Hierarchical.Frontiers in molecular biosciences · 2018Article
- Slow conformational exchange and overall rocking motion in ubiquitin protein crystals.Nature communications · 2017Article
- Measurement ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2017Article
- Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.Progress in nuclear magnetic resonance spectroscopy · 2016Review
- Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding.Nature communications · 2014Article
- Heteronuclear transverse and longitudinal relaxation in AX4 spin systems: application to (15)N relaxations in (15)NH4(+).Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Probing transient conformational states of proteins by solid-state R(1ρ) relaxation-dispersion NMR spectroscopy.Angewandte Chemie (International ed. in English) · 2014Article
- NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters.PloS one · 2014Article
- Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7.Nature chemical biology · 2013Article
- Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.Journal of the American Chemical Society · 2012Article
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5 authors.
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Abstract
The three-dimensional structures of macromolecules fluctuate over a wide range of time-scales. Separating the individual dynamic processes according to frequency is of importance in relating protein motions to biological function and stability. We present here a general NMR method for the specific characterization of microsecond motions at backbone positions in proteins even in the presence of other dynamics such as large-amplitude nanosecond motions and millisecond chemical exchange processes. The method is based on measurement of relaxation rates of four bilinear coherences and relies on the ability of strong continuous radio frequency fields to quench millisecond chemical exchange. The utility of the methodology is demonstrated and validated through two specific examples focusing on the thermo-stable proteins, ubiquitin and protein L, where it is found that small-amplitude microsecond dynamics are more pervasive than previously thought. Specifically, these motions are localized to alpha helices, loop regions, and regions along the rim of beta sheets in both of the proteins examined. A third example focuses on a 28 kDa ternary complex of the chaperone Chz1 and the histones H2A.Z/H2B, where it is established that pervasive microsecond motions are localized to a region of the chaperone that is important for stabilizing the complex. It is further shown that these motions can be well separated from extensive millisecond dynamics that are also present and that derive from exchange of Chz1 between bound and free states. The methodology is straightforward to implement, and data recorded at only a single static magnetic field are required.
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