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Search Publications by: Susana Marujo Teixeira (Assoc)

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Displaying 1 - 5 of 5

A Round-Robin Approach Provides a Detailed Assessment of Biomolecular Small-Angle Scattering Data Reproducibility and Yields Consensus Curves for Benchmarking.

November 1, 2022
Author(s)
Jill Trewhella, Patrice Vachette, Jan Bierma, Clement Blanchet, Emre Brookes, Srinivas Chakravarthy, Leonie Chatzimagas, Thomas Cleveland, Nathan Cowieson, Ben Crossett, Anthony P. Duff, Daniel Franke, Frank Gabel, Richard E. Gillilan, Melissa Graewert, Alexander Grishaev, Jules M. Guss, Michal Hammel, Jesse Hopkins, Qingqui Huang, Jochen S. Hub, Gregory L. Hura, Thomas C. Irving, Cy M. Jeffries, Cheol Jeong, Nigel Kirby, Susan N. Krueger, Anne Martel, Tsutomu Matsui, Na Li, Javier Perez, Lionel Porcar, Thierry Prange, Ivan Rajkovic, Mattia Rocco, Daniel J. Rosenberg, Timothy M. Ryan, Soenke Seifert, Hiroshi Sekiguchi, Dmitri Svergun, Susana C. Marujo Teixeira, Aurelien Thureau, Thomas M. Weiss, Andrew Whitten, Kathleen Wood, Xiaobing Zuo
Small-Angle Scattering (SAS) data from 5 candidate proteins (RNaseA, lysozyme, xylanase, urate oxidase and xylose isomerase) were measured on 12 Small-Angle X-ray Scattering (SAXS) and 4 Small-Angle Neutron Scattering (SANS) instruments. In total, more

In-situ Monitoring of Protein Unfolding/Structural States under Cold High-Pressure Stress

November 26, 2021
Author(s)
Diana Gomes, Susana C. Marujo Teixeira, Juscelino Leao, Vladimir Razinkov, Wei Qi, Miguel Rodrigues, Christopher Roberts
Biopharmaceutical formulations may be compromised by freezing, which has been attributed to protein conformational changes at a low temperature, and adsorption to ice−liquid interfaces. However, direct measurements of unfolding/conformational changes in

Membrane transporter dimerization driven by differential lipid solvation energetics of dissociated and associated states

April 7, 2021
Author(s)
Rahul Chadda, Nathan Bernhardt, Elizabeth Kelley, Susana Marujo Teixeira, Kacie Griffith, Alejandro Gil-Ley, Tugba Ozturk, Lauren Hughes, Ana Forsythe, Venkatramanan Krishnamani, Jose Faraldo-Gomez, Janice Robertson
Over two-thirds of integral membrane proteins of known structure assemble into oligomers. Yet, the forces that drive the association of these proteins remain to be delineated, as the lipid bilayer is a solvent environment that is both structurally and

Effect of Phosphorylation on a Human-like Osteopontin Peptide

April 25, 2017
Author(s)
Samuel Lenton, Marco Grimaldo, Felix Roosen-Runge, Frank Schreiber, Tommy Nylander, Roger Clegg, Carl Holt, Michael Hartlein, Victoria Garcia Sakai, Tilo Seydel, Susana C. Marujo Teixeira
Osteopontin is a disordered phosphoprotein that is expressed in many species and tissues and has a range of distinct functions. A notable property of more highly phosphorylated isoforms of osteopontin is their ability to sequester nanoclusters of calcium
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