Thomas G Chadwick

Works (3)

Updated: July 5th, 2023 15:55

2008 journal article

Characterization of magnetic and electronic properties of trimetallic nitride endohedral fullerenes by SQUID magnetometry and electron paramagnetic resonance

CHEMICAL PHYSICS LETTERS, 453(4-6), 233–237.

By: T. Smirnova n , A. Smirnov  n, T. Chadwick n & K. Walker*

Contributors: T. Smirnova n , A. Smirnov n , T. Chadwick n & K. Walker*

UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, ORCID, NC State University Libraries
Added: August 6, 2018

2007 journal article

Local polarity and hydrogen bonding inside the Sec14p phospholipid-binding cavity: High-field multi-frequency electron paramagnetic resonance studies

BIOPHYSICAL JOURNAL, 92(10), 3686–3695.

By: T. Smirnova n , T. Chadwick n, M. Voinov n, O. Poluektov *, J. Tol *, A. Ozarowski*, G. Schaaf *, M. Ryan *, V. Bankaitis *

Contributors: T. Smirnova n , T. Chadwick n, M. Voinov n, O. Poluektov *, J. Van Tol *, A. Ozarowski*, G. Schaaf *, M. Ryan *, V. Bankaitis *

MeSH headings : Binding Sites; Computer Simulation; Electron Spin Resonance Spectroscopy / methods; Hydrogen Bonding; Models, Chemical; Models, Molecular; Phospholipid Transfer Proteins / chemistry; Phospholipids / chemistry; Protein Binding; Saccharomyces cerevisiae Proteins / chemistry; Solvents / chemistry; Static Electricity
TL;DR: The data suggest the polarity gradient inside the Sec14p cavity is a significant contributor to the driving molecular forces for extracting a phospholipid from the bilayer and the enhanced g-factor resolution of EPR provides researchers with a spectroscopic tool to deconvolute two major contributions to the x-component of the nitroxide g-matrix: hydrogen-bond formation and local electrostatic effects. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018

2006 journal article

The chemistry of phospholipid binding by the Saccharomyces cerevisiae phosphatidylinositol transfer protein Sec14p as determined by EPR spectroscopy

JOURNAL OF BIOLOGICAL CHEMISTRY, 281(46), 34897–34908.

By: T. Smirnova n , T. Chadwick n, R. MacArthur n, O. Poluektov *, L. Song *, M. Ryan *, G. Schaaf *, V. Bankaitis *

MeSH headings : Binding Sites; Gene Expression Regulation; Models, Molecular; Molecular Structure; Phosphatidylcholines / chemistry; Phosphatidylcholines / metabolism; Phospholipid Transfer Proteins / chemistry; Phospholipid Transfer Proteins / metabolism; Phospholipids / chemistry; Phospholipids / metabolism; Protein Binding; Saccharomyces cerevisiae / metabolism; Saccharomyces cerevisiae Proteins / chemistry; Saccharomyces cerevisiae Proteins / metabolism; Spectrometry, Mass, Electrospray Ionization / methods
TL;DR: The application of EPR spectroscopy is described to probe the local dynamics and the electrostatic microenvironment of phosphatidylcholine bound by Sec14p in a soluble protein-PtdCho complex and suggests a headgroup-out orientation ofSec14p-bound PtdCho. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2025) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.