Zobrazeno 1 - 10 of 105 pro vyhledávání: '"Leonard J. Mueller"'
1
Akademický článek
Allosteric regulation of substrate channeling: Salmonella typhimurium tryptophan synthase
Autor: Rittik K. Ghosh, Eduardo Hilario, Chia-en A. Chang, Leonard J. Mueller, Michael F. Dunn
Publikováno v: Frontiers in Molecular Biosciences, Vol 9 (2022)
The regulation of the synthesis of L-tryptophan (L-Trp) in enteric bacteria begins at the level of gene expression where the cellular concentration of L-Trp tightly controls expression of the five enzymes of the Trp operon responsible for the synthes
Externí odkaz: https://doaj.org/article/08172a7fbefc40dbbe9feb15bd32ca11
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2
Akademický článek
Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools
Autor: Chia-en A. Chang, Yu-ming M. Huang, Leonard J. Mueller, Wanli You
Publikováno v: Catalysts, Vol 6, Iss 6, p 82 (2016)
This review discusses the use of molecular modeling tools, together with existing experimental findings, to provide a complete atomic-level description of enzyme dynamics and function. We focus on functionally relevant conformational dynamics of enzy
Externí odkaz: https://doaj.org/article/32cecf413a924d66ae034f82d4d87948
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3
A theoretical framework for the design of molecular crystal engines
Autor: Cameron J. Cook, Wangxiang Li, Brandon F. Lui, Thomas J. Gately, Rabih O. Al-Kaysi, Leonard J. Mueller, Christopher J. Bardeen, Gregory J. O. Beran
Publikováno v: Chemical science, vol 14, iss 4
Photomechanical molecular crystals have garnered attention for their ability to transform light into mechanical work, but difficulties in characterizing the structural changes and mechanical responses experimentally have hindered the development of p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4db4a732c0eac0d2d033be70ce4a589
https://doi.org/10.1039/d2sc05549j
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5
Discovery of antimicrobial agent targeting tryptophan synthase
Autor: Yuliana K. Bosken, Huanbin Zhou, Li Fan, Chia-en A. Chang, Wenbo Ma, Leonard J. Mueller, Shih-Hsin Kan, Rittik K. Ghosh, Eduardo Hilario, Michael F. Dunn, Dimitri Niks, Rizi Ai
Publikováno v: Protein Sci
Antibiotic and antimicrobial resistance is a continually growing challenge in the treatment of various bacterial infections worldwide. New drugs and new drug targets are necessary to curb the threat of infectious diseases caused by multidrug-resistan
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2ab6b00a07ca389633351a96410ff9e
https://doi.org/10.1002/pro.4236
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6
Bridging photochemistry and photomechanics with NMR crystallography: the molecular basis for the macroscopic expansion of an anthracene ester nanorod†
Autor: Joshua D. Hartman, Adam D. Gill, Ryan C. Hayward, Wenwen Xu, Kevin R. Chalek, Fei Tong, Lingyan Zhu, Alviclér Magalhães, Chen Yang, Richard J. Hooley, Xinning Dong, Leonard J. Mueller, Rabih O. Al-Kaysi, Gregory J. O. Beran, Ryan A. Kudla, Christopher J. Bardeen
Publikováno v: Chemical Science
Chemical science, vol 12, iss 1
Crystals composed of photoreactive molecules represent a new class of photomechanical materials with the potential to generate large forces on fast timescales. An example is the photodimerization of 9-tert-butyl-anthracene ester (9TBAE) in molecular
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfd49435b443e0cbfa583147c3401fd4
http://europepmc.org/articles/PMC8178812
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7
Non-Uniform Sampling in NMR Spectroscopy and the Preservation of Spectral Knowledge in the Time and Frequency Domains
Autor: Gabriel S. Phun, Manpreet Kaur, Leonard J. Mueller, Aaron M. Chronister, Callie M. Lewis
Publikováno v: J Phys Chem A
The increased sensitivity under weighted non-uniform sampling (NUS) is demonstrated and quantified using Monte Carlo simulations of nuclear magnetic resonance time- and frequency-domain signals. The concept of spectral knowledge is introduced and sho
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4a8f92c1b373558d18c8edaef1a90a0
https://doi.org/10.1021/acs.jpca.0c02930
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8
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR
Autor: Bethany G. Caulkins, Leonard J. Mueller, Varun V. Sakhrani, Mary E. Hatcher-Skeers, Michael F. Dunn, Li Fan, Eduardo Hilario
Publikováno v: Journal of biomolecular NMR, vol 74, iss 6-7
J Biomol NMR
Backbone assignments for the isolated α-subunit of Salmonella typhimurium tryptophan synthase (TS) are reported based on triple resonance solution-state NMR experiments on a uniformly (2)H,(13)C,(15)N-labeled sample. From the backbone chemical shift
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67af915dcdd343a7a0829e4bdfe1900a
https://doi.org/10.1007/s10858-020-00320-2
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9
Moderated Basicity of Endohedral Amine Groups in an Octa‐Cationic Self‐Assembled Cage
Autor: Courtney Ngai, Hoi‐Ting Wu, Bryce da Camara, Christopher G. Williams, Leonard J. Mueller, Ryan R. Julian, Richard J. Hooley
Publikováno v: Angew Chem Int Ed Engl
Angewandte Chemie (International ed. in English), vol 61, iss 11
A self-assembled Fe(II)(4)L(6) cage was synthesized with 12 internal amines in the cavity. The cage forms as the dodeca-ammonium salt, despite the cage carrying an overall 8+ charge at the metal centers, extracting protons from displaced water in the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1988ad0838cad2aa4fd41d0aaac5c629
https://doi.org/10.1002/anie.202117011
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10
Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate
Autor: Jacob B. Holmes, Viktoriia Liu, Bethany G. Caulkins, Eduardo Hilario, Rittik K. Ghosh, Victoria N. Drago, Robert P. Young, Jennifer A. Romero, Adam D. Gill, Paul M. Bogie, Joana Paulino, Xiaoling Wang, Gwladys Riviere, Yuliana K. Bosken, Jochem Struppe, Alia Hassan, Jevgeni Guidoulianov, Barbara Perrone, Frederic Mentink-Vigier, Chia-en A. Chang, Joanna R. Long, Richard J. Hooley, Timothy C. Mueser, Michael F. Dunn, Leonard J. Mueller
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 2
Proceedings of the National Academy of Sciences of the United States of America
Significance The determination of active site protonation states is critical for a full mechanistic understanding of enzymatic transformations. However, hydrogen atom positions are challenging to extract using the standard tools of structural biology
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08d7608d5aac5e21b95efa8324291114
https://doi.org/10.1073/pnas.2109235119
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