Cymal-4 - PMC

Aaron J. Wolfe, Wei Si, Zhengqi Zhang, Adam R. Blanden, Yi-Ching Hsueh, Jack F. Gugel, Bach Pham, Min Chen, Stewart N. Loh, Sharon Rozovsky, Aleksei Aksimentiev, Liviu Movileanu

J Phys Chem B. Author manuscript; available in PMC 2018 Nov 9.

Published in final edited form as: J Phys Chem B. 2017 Nov 9; 121(44): 10228–10241. Published online 2017 Oct 31. doi: 10.1021/acs.jpcb.7b08045

PMCID:: PMC5680101

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Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis

Catherine Vénien-Bryan, Carlos A. H. Fernandes

Int J Mol Sci. 2023 Oct; 24(19): 14785. Published online 2023 Sep 30. doi: 10.3390/ijms241914785

PMCID:: PMC10573263

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Expression and Purification of Human and Saccharomyces cerevisiae Equilibrative Nucleoside Transporters

Rebba C. Boswell-Casteel, Jennifer M. Johnson, Zygy Roe-ŽDurž, Kelli D. Duggan, Hannah Schmitz, Franklin A. Hays

Protein Expr Purif. Author manuscript; available in PMC 2019 Feb 1.

Published in final edited form as: Protein Expr Purif. 2018 Feb; 142: 68–74. Published online 2017 Sep 14. doi: 10.1016/j.pep.2017.09.002

PMCID:: PMC5679208

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High-Throughput Screening of Protein-Detergent Complexes Using Fluorescence Polarization Spectroscopy

Aaron J. Wolfe, Kyle J. Parella, Liviu Movileanu

Curr Protoc Protein Sci. Author manuscript; available in PMC 2020 Sep 1.

Published in final edited form as: Curr Protoc Protein Sci. 2019 Sep; 97(1): e96. doi: 10.1002/cpps.96

PMCID:: PMC6746331

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Small Amphipathic Molecules Modulate Secondary Structure and Amyloid Fibril-forming Kinetics of Alzheimer Disease Peptide Aβ_1–42

Timothy M. Ryan, Anna Friedhuber, Monica Lind, Geoffrey J. Howlett, Colin Masters, Blaine R. Roberts

J Biol Chem. 2012 May 11; 287(20): 16947–16954. Published online 2012 Mar 29. doi: 10.1074/jbc.M111.321778

PMCID:: PMC3351313

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Photoreverse Reaction Dynamics of Octopus Rhodopsin

Keiichi Inoue, Motoyuki Tsuda, Masahide Terazima

Biophys J. 2007 May 15; 92(10): 3643–3651. Published online 2007 Feb 26. doi: 10.1529/biophysj.106.101741

PMCID:: PMC1853134

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Analysis of Carotenoid Isomerase Activity in a Prototypical Carotenoid Cleavage Enzyme, Apocarotenoid Oxygenase (ACO)

Xuewu Sui, Philip D. Kiser, Tao Che, Paul R. Carey, Marcin Golczak, Wuxian Shi, Johannes von Lintig, Krzysztof Palczewski

J Biol Chem. 2014 May 2; 289(18): 12286–12299. Published online 2014 Mar 19. doi: 10.1074/jbc.M114.552836

PMCID:: PMC4007427

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Monitoring the function of membrane transport proteins in detergent-solubilized form

Matthias Quick, Jonathan A. Javitch

Proc Natl Acad Sci U S A. 2007 Feb 27; 104(9): 3603–3608. Published online 2007 Feb 20. doi: 10.1073/pnas.0609573104

PMCID:: PMC1805550

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Crystallization and preliminary X-ray crystallographic studies of human voltage-dependent anion channel isoform I (HVDAC1)

Thomas Meins, Clemens Vonrhein, Kornelius Zeth

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1; 64(Pt 7): 651–655. Published online 2008 Jun 28. doi: 10.1107/S174430910801676X

PMCID:: PMC2443964

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Expression, purification and crystallization of CTB-MPR, a candidate mucosal vaccine component against HIV-1

Ho-Hsien Lee, Irene Cherni, HongQi Yu, Raimund Fromme, Jeffrey D. Doran, Ingo Grotjohann, Michele Mittman, Shibom Basu, Arpan Deb, Katerina Dörner, Andrew Aquila, Anton Barty, Sébastien Boutet, Henry N. Chapman, R. Bruce Doak, Mark S. Hunter, Daniel James, Richard A. Kirian, Christopher Kupitz, Robert M. Lawrence, Haiguang Liu, Karol Nass, Ilme Schlichting, Kevin E. Schmidt, M. Marvin Seibert, Robert L. Shoeman, John C. H. Spence, Francesco Stellato, Uwe Weierstall, Garth J. Williams, Chunhong Yoon, Dingjie Wang, Nadia A. Zatsepin, Brenda G. Hogue, Nobuyuki Matoba, Petra Fromme, Tsafrir S. Mor

IUCrJ. 2014 Sep 1; 1(Pt 5): 305–317. Published online 2014 Aug 20. doi: 10.1107/S2052252514014900

PMCID:: PMC4174873

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Structural basis of the inhibition of cystathionine γ‐lyase from Toxoplasma gondii by propargylglycine and cysteine

Carmen Fernández‐Rodríguez, Carolina Conter, Iker Oyenarte, Filippo Favretto, Iban Quintana, Maria Luz Martinez‐Chantar, Alessandra Astegno, Luis Alfonso Martínez‐Cruz

Protein Sci. 2023 Apr; 32(4): e4619. Published online 2023 Apr 1. doi: 10.1002/pro.4619

PMCID:: PMC10053738

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Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis

Nirupa Nagaratnam, Jose M. Martin-Garcia, Jay-How Yang, Matthew R. Goode, Gihan Ketawala, Felicia M. Craciunescu, James D. Zook, Manashi Sonowal, Dewight Williams, Thomas D. Grant, Raimund Fromme, Debra T. Hansen, Petra Fromme

PLoS One. 2022; 17(8): e0267370. Published online 2022 Aug 1. doi: 10.1371/journal.pone.0267370

PMCID:: PMC9342783

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Interrogating Detergent Desolvation of Nanopore-Forming Proteins by Fluorescence Polarization Spectroscopy

Aaron J. Wolfe, Yi-Ching Hsueh, Adam R. Blanden, Mohammad M. Mohammad, Bach Pham, Avinash K. Thakur, Stewart N. Loh, Min Chen, Liviu Movileanu

Anal Chem. Author manuscript; available in PMC 2018 Aug 1.

Published in final edited form as: Anal Chem. 2017 Aug 1; 89(15): 8013–8020. Published online 2017 Jul 10. doi: 10.1021/acs.analchem.7b01339

PMCID:: PMC5558884

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Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin

Stephan Hirschi, David Kalbermatter, Zöhre Ucurum, Thomas Lemmin, Dimitrios Fotiadis

Nat Commun. 2021; 12: 4107. Published online 2021 Jul 5. doi: 10.1038/s41467-021-24429-6

PMCID:: PMC8257665

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High-throughput stability screening for detergent-solubilized membrane proteins

Vadim Kotov, Kim Bartels, Katharina Veith, Inokentijs Josts, Udaya K. Tiruttani Subhramanyam, Christian Günther, Jörg Labahn, Thomas C. Marlovits, Isabel Moraes, Henning Tidow, Christian Löw, Maria M. Garcia-Alai

Sci Rep. 2019; 9: 10379. Published online 2019 Jul 17. doi: 10.1038/s41598-019-46686-8

PMCID:: PMC6637136

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Translation of Chemical Structure into Dissipative Particle Dynamics Parameters for Simulation of Surfactant Self-Assembly

Ennio Lavagnini, Joanne L. Cook, Patrick B. Warren, Christopher A. Hunter

J Phys Chem B. 2021 Apr 22; 125(15): 3942–3952. Published online 2021 Apr 13. doi: 10.1021/acs.jpcb.1c00480

PMCID:: PMC8154614

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Structure Analysis of the Proteins Associated with PolyA Repeat Expansion Disorders

Rolando Hernandez, Julio C. Facelli

J Biomol Struct Dyn. Author manuscript; available in PMC 2023 Aug 1.

Published in final edited form as: J Biomol Struct Dyn. 2022 Aug; 40(12): 5556–5565. Published online 2021 Jan 18. doi: 10.1080/07391102.2021.1871957

PMCID:: PMC8286276

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Figure 4:Time-dependent FP anisotropy showing the CYMAL-4 desolvation of OmpG at various pH values.

The starting CYMAL-4 concentration was 50 mM. (A) pH 4.6; (B) pH 5.6; (C) pH 6.8; (D) pH 8.2; (E) pH 10.0. The other experimental conditions were the same as those stated in the caption of .

Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics

J Phys Chem B. ;122(41):9471-9481.
Figure 8:Dependence of the observed desolvation rate constants, , on the protein charge.

(A) The values were determined for the DM desolvation of FhuA ΔC/Δ5L, FhuA ΔC/Δ5L_25N, and FhuA ΔC/Δ7L_30N at 1 mM DM; (B) The values were determined for the DM desolvation of FhuA ΔC/Δ5L, FhuA ΔC/Δ5L_25N, and FhuA ΔC/Δ7L_30N at 0.85 mM DM; (C) The values were determined for the CYMAL-4 desolvation of FhuA ΔC/Δ5L, FhuA ΔC/Δ5L_25N, and FhuA ΔC/Δ7L_30N at pH 8.2. Different vertical columns show data acquired at various CYMAL-4 concentrations; (D) Illustration of the initial desolvation rates, , which were determined for proteins of varying overall charge at pH 8.2. The final detergent concentrations for DM and CYMAL-4 were 1 and 4 mM, respectively. The other experimental conditions were the same as those stated in the caption of .

Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics

J Phys Chem B. ;122(41):9471-9481.
FIGURE 3.

Electron microscope images of Aβ_1–42 solutions containing activating detergents (deoxycholate (A), octyl-β-d-thioglucoside (B), FOS-choline-8 (C), CYMAL-4 (D), thesit (E), and n-decanoylsucrose (F)).

Small Amphipathic Molecules Modulate Secondary Structure and Amyloid Fibril-forming Kinetics of Alzheimer Disease Peptide Aβ1–42

J Biol Chem. 2012 May 11;287(20):16947-16954.
FIGURE 4.

Concentration dependence of the effects of activating detergents (deoxycholate (A), octyl-β-d-thioglucoside (B), FOS-choline-8 (C), CYMAL-4 (D), thesit (E), and n-decanoylsucrose (F)). Error bars are ± Standard deviation.

Small Amphipathic Molecules Modulate Secondary Structure and Amyloid Fibril-forming Kinetics of Alzheimer Disease Peptide Aβ1–42

J Biol Chem. 2012 May 11;287(20):16947-16954.