Zobrazeno 1 - 10 of 14 pro vyhledávání: '"Adam M. Zmyslowski"'
1
Development of in vivo HDX-MS with applications to a TonB-dependent transporter and other proteins
Autor: Xiaoxuan Lin, Adam M. Zmyslowski, Isabelle A. Gagnon, Robert K. Nakamoto, Tobin R. Sosnick
Publikováno v: Protein science : a publication of the Protein Society. 31(9)
Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is a powerful tool that monitors protein dynamics in solution. However, the reversible nature of HDX labels has largely limited the application to in vitro systems. Here, we describe a protocol f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c15ff1243f1867a210c08fd59dc4798a
https://pubmed.ncbi.nlm.nih.gov/36040258
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2
HDX-MS performed on BtuB in
Autor: Adam M, Zmyslowski, Michael C, Baxa, Isabelle A, Gagnon, Tobin R, Sosnick
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 119(20)
To import large metabolites across the outer membrane of gram-negative bacteria, TonB-dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the Escherichia coli vitamin B12 TBDT, TonB binds and cou
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dd87f6c39e74faa0ba0a0dbfd9e698ad
https://pubmed.ncbi.nlm.nih.gov/35549554
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3
HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain’s allostery and unfolding upon B12 and TonB binding
Autor: Adam M. Zmyslowski, Michael C. Baxa, Isabelle A. Gagnon, Tobin R. Sosnick
To import large metabolites across the outer membrane of Gram-negative bacteria, TonB dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the E. coli vitamin B12 TBDT, TonB binds and couples BtuB
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::158829da09b552be03d8d168efaffb63
https://doi.org/10.1101/2022.01.07.475440
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5
Commonly used FRET fluorophores promote collapse of an otherwise disordered protein
Autor: Micayla A. Bowman, Adam M. Zmyslowski, Joshua A. Riback, Tobin R. Sosnick, Kevin W. Plaxco, Patricia L. Clark
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 18
The dimensions that unfolded proteins, including intrinsically disordered proteins (IDPs), adopt in the absence of denaturant remain controversial. We developed an analysis procedure for small-angle X-ray scattering (SAXS) profiles and used it to dem
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44dc130c65218e954185813d9c00818
https://doi.org/10.1073/pnas.1813038116
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6
Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water
Autor: Karl F. Freed, John M. Jumper, Adam M. Zmyslowski, Micayla A. Bowman, Tobin R. Sosnick, Emily B. Kaye, Joshua A. Riback, James R. Hinshaw, Catherine R. Knoverek, Patricia L. Clark
Publikováno v: Science
An expanded view of disordered proteins Disordered proteins sample an ensemble of conformations, but it has remained unclear how compact these conformations are in water. Polymer physics relates the radius of gyration ( R g ) to solvent quality, with
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15bac96d64670b9e2188a08b9424e476
https://doi.org/10.1126/science.aan5774
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7
Commonly-used FRET fluorophores promote collapse of an otherwise disordered protein
Autor: Kevin W. Plaxco, Micayla A. Bowman, Adam M. Zmyslowski, Tobin R. Sosnick, Patricia L. Clark, Joshua A. Riback
The dimensions that unfolded and intrinsically disordered proteins (IDPs) adopt at low or no denaturant remains controversial. We recently developed an innovative analysis procedure for small-angle X-ray scattering (SAXS) profiles and found that even
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04fb2f9fe586c3f142dcaa17e53d7119
https://doi.org/10.1101/376632
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8
Response to Comment on 'Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water'
Autor: Micayla A. Bowman, Emily B. Kaye, Karl F. Freed, John M. Jumper, Adam M. Zmyslowski, Catherine R. Knoverek, Tobin R. Sosnick, Patricia L. Clark, Joshua A. Riback
Publikováno v: Science
Best et al . claim that we provide no convincing basis to assert that a discrepancy remains between FRET and SAXS results on the dimensions of disordered proteins under physiological conditions. We maintain that a clear discrepancy is apparent in our
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dc74001727a1fe944a61cf3b4960780
https://pubmed.ncbi.nlm.nih.gov/30166459
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9
Structural Basis for Multi-specificity of MRG Domains
Autor: Ishwar Radhakrishnan, Adam M. Zmyslowski, Tao Xie, Yongbo Zhang
Publikováno v: Structure. 23(6):1049-1057
Chromatin-binding proteins play vital roles in the assembly and recruitment of multi-subunit complexes harboring effector proteins to specific genomic loci. MRG15, a chromodomain-containing chromatin-binding protein, recruits diverse chromatin-associ
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a168c8d4c1c9c3ef6fe2dd3c63e6017
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