A molten globule ensemble primes Arf1-GDP for the nucleotide switch.

Autor: Koduru T; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180., Hantman N; Graduate Program in Biochemistry and Biophysics, School of Science, Rensselaer Polytechnic Institute, Troy, NY 12180., Peters EV; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180., Jaworek MW; Department of Chemistry and Chemical Biology, Biophysical Chemistry, Technical University of Dortmund University, Dortmund D-44227, Germany., Wang J; Graduate Program in Biochemistry and Biophysics, School of Science, Rensselaer Polytechnic Institute, Troy, NY 12180., Zhang S; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180., McCallum SA; Shirley Ann Jackson, PhD. Center for Biotechnology and Interdisciplinary Science, Rensselaer Polytechnic Institute, Troy, NY 12180., Gillilan RE; Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853., Fossat MJ; Department of Biological Physics, Max Planck Institute of Immunobiology and Epigenetic, Freiburg D-79108, Germany., Roumestand C; Centre de Biochimie Structurale, CNRS, INSERM, Université de Montpellier, Montpellier 34090, France., Sagar A; Centre de Biochimie Structurale, CNRS, INSERM, Université de Montpellier, Montpellier 34090, France., Winter R; Department of Chemistry and Chemical Biology, Biophysical Chemistry, Technical University of Dortmund University, Dortmund D-44227, Germany., Bernadó P; Centre de Biochimie Structurale, CNRS, INSERM, Université de Montpellier, Montpellier 34090, France., Cherfils J; Université Paris-Saclay, Ecole Normale Supérieure Paris-Saclay, CNRS, Gif-sur-Yvette 91190, France., Royer CA; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Sep 24; Vol. 121 (39), pp. e2413100121. Date of Electronic Publication: 2024 Sep 18.

Macromolecular condensation organizes nucleolar sub-phases to set up a pH gradient.

Autor: King MR; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Ruff KM; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Lin AZ; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Pant A; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Farag M; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Lalmansingh JM; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Wu T; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Department of Electrical and Systems Engineering, James F. McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA., Fossat MJ; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Ouyang W; Department of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, CA, USA; Department of Pathology, School of Medicine, Stanford University, Stanford, CA, USA; Science for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH-Royal Institute of Technology, Stockholm, Sweden., Lew MD; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Department of Electrical and Systems Engineering, James F. McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA., Lundberg E; Department of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, CA, USA; Department of Pathology, School of Medicine, Stanford University, Stanford, CA, USA; Science for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH-Royal Institute of Technology, Stockholm, Sweden., Vahey MD; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA., Pappu RV; Department of Biomedical Engineering, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA. Electronic address: pappu@wustl.edu.

Publikováno v: Cell [Cell] 2024 Apr 11; Vol. 187 (8), pp. 1889-1906.e24. Date of Electronic Publication: 2024 Mar 18.

Quantifying charge state heterogeneity for proteins with multiple ionizable residues.

Autor: Fossat MJ; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, Missouri., Posey AE; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, Missouri., Pappu RV; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, Missouri. Electronic address: pappu@wustl.edu.

Publikováno v: Biophysical journal [Biophys J] 2021 Dec 21; Vol. 120 (24), pp. 5438-5453. Date of Electronic Publication: 2021 Nov 23.

Design of intrinsically disordered proteins that undergo phase transitions with lower critical solution temperatures.

Autor: Zeng X; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA., Liu C; Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA., Fossat MJ; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA., Ren P; Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA., Chilkoti A; Department of Biomedical Engineering, Duke University, Durham, NC 27708, USA., Pappu RV; Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA.

Publikováno v: APL materials [APL Mater] 2021 Feb; Vol. 9 (2). Date of Electronic Publication: 2021 Feb 18.

The consequences of cavity creation on the folding landscape of a repeat protein depend upon context.

Autor: Jenkins KA; Graduate Program in Biochemistry and Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180., Fossat MJ; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180., Zhang S; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180., Rai DK; Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853., Klein S; T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218., Gillilan R; Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853., White Z; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180., Gerlich G; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180., McCallum SA; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180., Winter R; Department of Physical Chemistry, Technical University of Dortmund, 44227 Dortmund, Germany., Gruner SM; Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853.; Department of Physics, Cornell University, Ithaca, NY 14853.; Kavli Institute at Cornell for Nanoscale Science, Cornell University, Ithaca, NY 14853., Barrick D; T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218., Royer CA; Graduate Program in Biochemistry and Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180; royerc@rpi.edu.; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180.; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2018 Aug 28; Vol. 115 (35), pp. E8153-E8161. Date of Electronic Publication: 2018 Aug 13.