The dynamic interactions of enzymes and substrates underpins catalysis, yet few techniques can interrogate the dynamics of protein-bound ligands. Here we describe the use of field cycling NMR relaxometry to measure the dynamics of enzyme-bound substrates and cofactors in catalytically competent complexes of GMP reductase. These studies reveal new binding modes unanticipated by x-ray crystal structures and reaction-specific dynamic networks. Importantly, this work demonstrates that distal...
[NMR paper] High Resolution NMR H/D Exchange of Human Superoxide Dismutase Inclusion Bodies Reveals Significant Native Features Despite Structural Heterogeneity
High Resolution NMR H/D Exchange of Human Superoxide Dismutase Inclusion Bodies Reveals Significant Native Features Despite Structural Heterogeneity
Protein aggregation is central to aging, disease and biotechnology. While there has been recent progress in defining structural features of cellular protein aggregates, many aspects remain unclear due to heterogeneity of aggregates presenting obstacles to characterization. Here we report high-resolution analysis of cellular inclusion bodies (IBs) of immature human superoxide dismutase (SOD1) mutants using NMR quenched amide hydrogen/deuterium...
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[ASAP] Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution 31P Field-Cycling NMR Relaxometry
Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution 31P Field-Cycling NMR Relaxometry
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00142/20180326/images/medium/bi-2018-00142a_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00142
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03-27-2018 06:28 AM
[NMR paper] Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Biochemistry. 2018 Mar 16;:
Authors: Rosenberg MM, Redfield AG, Roberts M, Hedstrom L
Abstract
The ability of enzymes to modulate the dynamics of bound substrates and cofactors is a critical feature of catalysis, but the role of dynamics has largely been approached from the perspective of the protein....
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03-17-2018 12:12 PM
[NMR paper] High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
J Biol Chem. 2017 May 12;292(19):8082-8091
Authors: Kerkour A,...
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07-14-2017 01:53 PM
[NMR paper] Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.
Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.
Related Articles Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.
J Biol Chem. 2016 Sep 9;
Authors: Rosenberg MM, Redfield AG, Roberts MF, Hedstrom L
Abstract
Guanosine-5'-monophosphate reductase (GMPR) catalyzes the reduction of GMP to IMP and ammonia with concomitant oxidation of NADPH. Here we investigated the structure...
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09-22-2016 06:31 AM
[NMR paper] NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Related Articles NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Nat Commun. 2013;4:1890
Authors: Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercík K, Hritz J, Charlton LM, Levin JG, Gronenborn AM
Abstract
Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its...
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05-23-2013 06:54 PM
High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument
High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument
Abstract Improvements are described in a shuttling field-cycling device (Redfield in Magn Reson Chem 41:753â??768, 2003), designed to allow widespread access to this useful technique by configuring it as a removable module to a commercial 500 MHz NMR instrument. The main improvements described here, leading to greater versatility, high reliability and simple construction, include: shuttling provided by a linear motor driven by an integrated-control...
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12-31-2011 10:40 AM
[NMR paper] High-resolution 31p field cycling NMR as a probe of phospholipid dynamics.
High-resolution 31p field cycling NMR as a probe of phospholipid dynamics.
Related Articles High-resolution 31p field cycling NMR as a probe of phospholipid dynamics.
J Am Chem Soc. 2004 Oct 27;126(42):13765-77
Authors: Roberts MF, Redfield AG
We have used high-resolution field-cycling 31P NMR spectroscopy to measure spin-lattice relaxation rates (R1 = 1/T1) of multicomponent phospholipid vesicle and micelle samples over a large field range, from 0.1 to 11.7 T. The shape of the curve for R1 as a function of field and a model-free analysis were...
High Resolution 31P Field Cycling NMR Reveals Unsuspected Features of Enzyme-Substrate-Cofactor Dynamics
Linear Mode
