(Q30405801)

English

Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR.

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scholarly article

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Europe PubMed Central

PubMed publication ID

21 June 2017

Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. (English)

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

author name string

Philippe S Nadaud

1

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

Ishita Sengupta

2

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

Jonathan J Helmus

3

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

Christopher P Jaroniec

4

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

publication date

9 August 2011

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

Journal of Biomolecular NMR

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Europe PubMed Central

PubMed publication ID

21 June 2017

51

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

293-302

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

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High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein

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Prions: En route from structural models to structures

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Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.

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Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy

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Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy

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Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR.

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Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins.

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Rapid acquisition of multidimensional solid-state NMR spectra of proteins facilitated by covalently bound paramagnetic tags.

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Protein NMR using paramagnetic ions

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Solid-state NMR spectroscopy on complex biomolecules

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The Xplor-NIH NMR molecular structure determination package

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Relaxation Processes in a System of Two Spins

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Solid-state NMR studies of amyloid fibril structure

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Paramagnetic resonance of biological metal centers

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Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries

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A new approach in 1D and 2D 13C high-resolution solid-state NMR spectroscopy of paramagnetic organometallic complexes by very fast magic-angle spinning

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Fast acquisition of multi-dimensional spectra in solid-state NMR enabled by ultra-fast MAS

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Structural information on a membrane transport protein from nuclear magnetic resonance spectroscopy using sequence-selective nitroxide labeling

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Solid-state NMR fermi contact and dipolar shifts in organometallic complexes and metalloporphyrins

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Perspectives in paramagnetic NMR of metalloproteins

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Transverse-Dephasing Optimized HomonuclearJ-Decoupling in Solid-State NMR Spectroscopy of Uniformly13C-Labeled Proteins

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Solid-State NMR Spectroscopy of a Paramagnetic Protein: Assignment and Study of Human Dimeric Oxidized CuII–ZnII Superoxide Dismutase (SOD)

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Paramagnetic Ions Provide Structural Restraints in Solid-State NMR of Proteins

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Ultrafast MAS Solid-State NMR Permits Extensive13C and1H Detection in Paramagnetic Metalloproteins

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Nuclear magnetic resonance of hemeprotein crystals. Structure of the heme in Physeter catodon ferrimyoglobin and an analysis of hyperfine shifts.

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Short selective pulses for biochemical applications

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Incorporation of an EDTA-metal complex at a rationally selected site within a protein: application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro

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Spin labeling of proteins

1 reference

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Long-range structural restraints in spin-labeled proteins probed by solid-state nuclear magnetic resonance spectroscopy

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Identifiers

10.1007/S10858-011-9536-Y

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

ResearchGate publication ID

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