Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Protein Sci. 2011 Feb;20(2):229-46
Authors: Clore GM
Sparsely populated states of macromolecules, characterized by short lifetimes and high free-energies relative to the predominant ground state, often play a key role in many biological, chemical, and biophysical processes. In this review, we briefly summarize various new developments in NMR spectroscopy that permit these heretofore invisible, sparsely populated states to be detected, characterized, and in some instances visualized. Relaxation dispersion spectroscopy yields detailed kinetic information on processes involving species characterized by distinct chemical shifts with lifetimes in the ~50 ?s-10 ms range and populations as low as 0.5%. In the fast exchange regime (time scale less than ~250-500 ?s), the footprint of sparsely populated states can be observed on paramagnetic relaxation enhancement profiles measured on the resonances of the major species, thereby yielding structural information that is directly related to paramagnetic center-nuclei distances from which it is possible, under suitable circumstances, to compute a structure or ensemble of structures for the minor species. Finally, differential transverse relaxation measurements can be used to detect lifetime broadening effects that directly reflect the unidirectional rates for the conversion of NMR-visible into high-molecular weight NMR-invisible species. Examples of these various approaches are presented.
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-29-2011 04:45 AM
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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06-07-2011 11:05 AM
[NMR paper] Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Related Articles Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Nature. 2004 Jul 29;430(6999):586-90
Authors: Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE
Many biochemical processes proceed through the formation of functionally significant intermediates. Although the identification and characterization of such species can provide vital clues about the mechanisms of the...
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11-24-2010 09:51 PM
[NMR paper] Determination of the electron relaxation rates in paramagnetic metal complexes: appli
Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.
Related Articles Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.
J Magn Reson. 2004 Apr;167(2):169-77
Authors: Jensen MR, Led JJ
Four different approaches for determining the electron relaxation rates in paramagnetic metallo-proteins are investigated, using a paramagnetic Ni2+ complex of a protein as an example. All four approaches rely on the...
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11-24-2010 09:51 PM
[NMR paper] Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Related Articles Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
J Am Chem Soc. 2001 May 2;123(17):3953-9
Authors: Baber JL, Szabo A, Tjandra N
The interpretation of NMR relaxation data for macromolecules possessing slow interdomain motions is considered. It is shown how the "extended model-free approach" can be used to analyze (15)N backbone relaxation data acquired at three different field strengths for Xenopus Ca(2+)-ligated...
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11-19-2010 08:32 PM
[Question from NMRWiki Q&A forum] Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NM
Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NMR
I am a beginner in NMR spectroscopy and I would like to learn more about relaxation editing experiments vs PRE. A colleague of mine is doing the 13C CP-MAS NMR experim. and he using cellulose II powder, regenerated cellulose and milled reg cellulose. We are interested in C4 resonance of cellulose II, good resolved resonance, to better understand the supramolecular structure of cellulose II. As experiments: long relaxation experiments - PRE with aqueous CuSO4 solution of certain concentration, does the...
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10-15-2010 05:16 PM
[Question from NMRWiki Q&A forum] Does anyone know something about paramagnetic relaxation enhancement (PRE)?
Does anyone know something about paramagnetic relaxation enhancement (PRE)?
Does anyone know something about paramagnetic relaxation enhancement (PRE)? i would like to try this method on my cellulose materials. What info can you take out of it? Thank you very much.
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09-08-2010 12:08 AM
Tunable paramagnetic relaxation enhancements by [Gd(DPA)3]3â?? for protein structure
Abstract Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and proteinâ??ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, 3â??, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of 3â?? to protein, allowing quantitative distance measurements for nuclear spins...
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
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