Theory, Practice and Applications of Paramagnetic Relaxation Enhancement for the Characterization of Transient Low-Population States of Biological Macromolecules and Their Complexes
By G. Clore, J. Iwahara. Chemical Reviews, 2009
695 citations recorded by the source corpus.
Understanding the function of biological macromolecules and their complexes at the physicochemical level requires knowledge of both their structure and dynamics. Conventional biophysical techniques, such as crystallography and NMR, have yielded incredibly detailed structural information at the atomic level on highly populated static states.1 In the context of the energy landscape representation of macromolecules, highly populated states are located within the global free energy minimum region of a relatively rough free energy hypersurface.2-5 Much less is known, however, about lowly populated, higher free energy states which cannot be * E-mail: G.M.C., mariusc@mail.nih.gov; J.I., j.iwahara@utmb.edu. † National Institutes of Health. ‡ University of Texas Medical Branch. Chem. Rev. 2009, 109, 4108–4139 4108
Subfields: Biophysics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/19a562ebed8e3bbda516d82502552104b2af34a7
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In Biophysics
In Molecular Biology
- Santrupti Nerli
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- Andrew C. McShan
- Julia Koehler Leman
- Richard Bonneau
- Georg Kuenze
- Jens Meiler
- Martin Blackledge
Citations in the corpus
- CS-ROSETTA (2018, methodology): “…restraints are typically provided by NMR chemical shifts and NOEs (Anglister, Srivastava, & Naider, 2016; Güntert, 2009), whereas global information is obtained from RDC (Blackledge, 2005), PCS (pseudocontact shift) and PRE (paramagnetic relaxation enhancement) (Clore & Iwahara, 2009) restraints.”
- Integrative protein modeling in RosettaNMR from sparse paramagnetic restraints (2019, background): “In addition, PCSs exhibit a more favorable r −3 distance dependence (r −6 for PREs) and are less affected by the presence of minor protein states or encounter complexes (Clore and Iwahara, 2009).”
- Chemical shift-based methods in NMR structure determination (2018, background): “Thus, hybrid approaches that combine chemical shifts with additional shortrange and long-range restraints, such as NOE [219], RDC [220], PRE [221], and PCS [221] measurements, are expected to further increase the scope, accuracy and resolution of NMR derived structures.”
- Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables (2012, methodology): “J(ω) can be described using a model-free expression of the order parameter, comprising the orientational and distance-dependent components of the internal motion that both strongly depend on the motion of the spin label with respect to the observed nuclear spin (Bruschweiler et al., 1992; Clore and ”