Active Filters

  • (-) Keywords = protein
Search Results 1 - 13 of 13
  • RSS Feed
Select Page
Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals
Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., … Abrahams, J. P. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology, 77, 75-85. https://doi.org/10.1107/S2059798320014540
Fabrication of a novel protein sponge with dual-scale porosity and mixed wettability using a clean and versatile microwave-based process
Wemmer, J., Malafronte, L., Foschini, S., Schneider, A., Schlepütz, C. M., Leser, M. E., … Windhab, E. J. (2021). Fabrication of a novel protein sponge with dual-scale porosity and mixed wettability using a clean and versatile microwave-based process. Materials, 14(9), 2298 (14 pp.). https://doi.org/10.3390/ma14092298
Characterization of MCU-binding proteins MCUR1 and CCDC90B — representatives of a protein family conserved in prokaryotes and eukaryotic organelles
Adlakha, J., Karamichali, I., Sangwallek, J., Deiss, S., Bär, K., Coles, M., … Hernandez Alvarez, B. (2019). Characterization of MCU-binding proteins MCUR1 and CCDC90B — representatives of a protein family conserved in prokaryotes and eukaryotic organelles. Structure, 27(3), 464-475.e6. https://doi.org/10.1016/j.str.2018.11.004
Direct observation of the Zr<sup>IV</sup> interaction with the carboxamide bond in a noncovalent complex between Hen Egg White Lysozyme and a Zr-substituted Keggin polyoxometalate
Vandebroek, L., Van Meervelt, L., & Parac-Vogt, T. N. (2018). Direct observation of the ZrIV interaction with the carboxamide bond in a noncovalent complex between Hen Egg White Lysozyme and a Zr-substituted Keggin polyoxometalate. Acta Crystallographica Section C: Structural Chemistry, 74(11), 1348-1354. https://doi.org/10.1107/S2053229618010690
Neutravidin-mediated extraction of isolated small diameter single walled carbon nanotubes for bio-recognition
Su, J., Wang, H., Wu, K., Liu, Z., Yin, Q., Wang, R., … Abrahams, J. P. (2017). Neutravidin-mediated extraction of isolated small diameter single walled carbon nanotubes for bio-recognition. Journal of Nanoscience and Nanotechnology, 17(5), 3588-3596. https://doi.org/10.1166/jnn.2017.12860
Poly-acrylic acid brushes and adsorbed proteins
Reinhardt, M., Kreuzer, M., Geue, T., Dahint, R., Ballauff, M., & Steitz, R. (2015). Poly-acrylic acid brushes and adsorbed proteins. Zeitschrift für Physikalische Chemie, 229(7-8), 1119-1139. https://doi.org/10.1515/zpch-2014-0540
Detection of protein structure of frozen ancient human remains recovered from a glacier in Canada using synchrotron Fourier transform infrared microspectroscopy
Quaroni, L., Christensen, C. R., Chen, B., Vogl, W., & Monsalve, M. V. (2013). Detection of protein structure of frozen ancient human remains recovered from a glacier in Canada using synchrotron Fourier transform infrared microspectroscopy. Microscopy and Microanalysis, 19(3), 565-575. https://doi.org/10.1017/S1431927613000615
SANS study of Lysozyme vs. BSA protein adsorption on silica nanoparticles
Kumar, S., Aswal, V. K., & Kohlbrecher, J. (2012). SANS study of Lysozyme vs. BSA protein adsorption on silica nanoparticles. In AIP conference proceedings: Vol. 1447. Solid state physics (pp. 181-182). https://doi.org/10.1063/1.4709940
Transient DNA/RNA-protein interactions
Blanco, F. J., & Montoya, G. (2011). Transient DNA/RNA-protein interactions. FEBS Journal, 278(10), 1643-1650. https://doi.org/10.1111/j.1742-4658.2011.08095.x
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Gruene, T., Cho, M. K., Karyagina, I., Kim, H. Y., Grosse, C., Giller, K., … Becker, S. (2011). Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy. Journal of Biomolecular NMR, 49(2), 111-119. https://doi.org/10.1007/s10858-011-9471-y
Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA
Melero, R., Rajagopalan, S., Lázaro, M., Joerger, A. C., Brandt, T., Veprintsev, D. B., … Valle, M. (2010). Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA. Proceedings of the National Academy of Sciences of the United States of America PNAS, 108(2), 557-562. https://doi.org/10.1073/pnas.1015520107
Crystal growth of proteins, nucleics acids, and viruses in gels
Lorber, B., Sauter, C., Théobald-Dietrich, A., Moreno, A., Schellenberger, P., Robert, M. C., … Giegé, R. (2009). Crystal growth of proteins, nucleics acids, and viruses in gels. Progress in Biophysics and Molecular Biology, 101(1-3), 13-25. https://doi.org/10.1016/j.pbiomolbio.2009.12.002
Time evolution of crystallization phase of lysozyme protein in aqueous salt solution as studied by scattering techniques
Chodankar, S., Aswal, V. K., Kohlbrecher, J., Hassan, P. A., & Wagh, A. G. (2007). Time evolution of crystallization phase of lysozyme protein in aqueous salt solution as studied by scattering techniques. Physica B: Condensed Matter, 398(1), 164-171. https://doi.org/10.1016/j.physb.2007.05.013