Visualizing transient dark states by NMR spectroscopy.
Q Rev Biophys. 2015 Feb;48(1):35-116
Authors: Anthis NJ, Clore GM
Abstract
Myriad biological processes proceed through states that defy characterization by conventional atomic-resolution structural biological methods. The invisibility of these 'dark' states can arise from their transient nature, low equilibrium population, large molecular weight, and/or heterogeneity. Although they are invisible, these dark states underlie a range of processes, acting as encounter complexes between proteins and as intermediates in protein folding and aggregation. New methods have made these states accessible to high-resolution analysis by nuclear magnetic resonance (NMR) spectroscopy, as long as the dark state is in dynamic equilibrium with an NMR-visible species. These methods - paramagnetic NMR, relaxation dispersion, saturation transfer, lifetime line broadening, and hydrogen exchange - allow the exploration of otherwise invisible states in exchange with a visible species over a range of timescales, each taking advantage of some unique property of the dark state to amplify its effect on a particular NMR observable. In this review, we introduce these methods and explore two specific techniques - paramagnetic relaxation enhancement and dark state exchange saturation transfer - in greater detail.
PMID: 25710841 [PubMed - as supplied by publisher]
[NMR paper] Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Angew Chem Int Ed Engl. 2014 Apr 22;53(17)
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J,...
nmrlearner
Journal club
0
04-23-2014 06:31 PM
[NMR paper] Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Related Articles Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Mar 18;
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P
Abstract
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally...
nmrlearner
Journal club
0
03-20-2014 12:44 PM
[NMR paper] Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Related Articles Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Biochim Biophys Acta. 2013 Dec 4;
Authors: Zhang Z, Dai C, Bai J, Xu G, Liu M, Li C
Abstract
?-synuclein is involved in Parkinson's disease and its interaction with cell membrane is crucial to its pathological and physiological functions. Membrane properties, such as curvature, lipid composition have been shown to affect the...
nmrlearner
Journal club
0
12-10-2013 05:36 PM
[NMR paper] Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Proc Natl Acad Sci U S A. 2013 Jun 24;
Authors: Libich DS, Fawzi NL, Ying J, Clore GM
Abstract
nmrlearner
Journal club
0
06-27-2013 02:10 PM
[NMR paper] Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applica
Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applications to real-time protein folding.
Related Articles Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applications to real-time protein folding.
J Am Chem Soc. 2003 Oct 15;125(41):12484-92
Authors: Mok KH, Nagashima T, Day IJ, Jones JA, Jones CJ, Dobson CM, Hore PJ
We describe the development and application of a novel rapid sample-mixing technique for real-time NMR (nuclear magnetic resonance) spectroscopy. The apparatus consists...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Biochemistry. 2003 Jun 17;42(23):7068-76
Authors: Worrall JA, Reinle W, Bernhardt R, Ubbink M
The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Abstract Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such transient intermediates in a number of protein-protein and protein-DNA complexes. Here we present an analysis of the recently published PRE NMR data for a protein complex of yeast...
nmrlearner
Journal club
0
11-06-2010 01:24 PM
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
J Biomol NMR. 2010 Nov 4;
Authors: Volkov AN, Ubbink M, van Nuland NA
Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such...