Výsledky vyhledávání - "Kurtis M. Anderson"

A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 + groups forming intermolecular ion pairs in protein–nucleic acid complexes

Autor: Kurtis M. Anderson, David G. Gorenstein, Levani Zandrashvili, Dan Nguyen, Alexandre Esadze, Junji Iwahara

Publikováno v: Journal of Biomolecular NMR. 62:1-5

Protein–nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three protein–DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allow

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::79efa3ace949177daa468c4f92ad6972
https://doi.org/10.1007/s10858-015-9909-8

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A chemical approach for site-specific identification of NMR signals from protein side-chain NH₃⁺ groups forming intermolecular ion pairs in protein-nucleic acid complexes

Autor: Kurtis M, Anderson, Dan, Nguyen, Alexandre, Esadze, Levani, Zandrashvili, David G, Gorenstein, Junji, Iwahara

Publikováno v: Journal of biomolecular NMR. 62(1)

Protein-nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three protein-DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allows fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1890488cae9ffbc7aa9a828979b2b203
https://pubmed.ncbi.nlm.nih.gov/25690740

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Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy

Autor: Kurtis M. Anderson, Alexandre Esadze, David G. Gorenstein, Mariappan Manoharan, Junji Iwahara, Rafael Brüschweiler

Publikováno v: Journal of the American Chemical Society. 135(9)

Ion pairing is one of the most fundamental chemical interactions and is essential for molecular recognition by biological macromolecules. From an experimental standpoint, very little is known to date about ion-pair dynamics in biological macromolecul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26961f9e3f3d863872d49d47071e9a26
https://pubmed.ncbi.nlm.nih.gov/23406569

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Oxygen-to-Sulfur Substitution of DNA Phosphate Entropically Enhances Protein-DNA Affinity

Autor: Dan Nguyen, David G. Gorenstein, Kurtis M. Anderson, Levani Zandarashvili, Junji Iwahara, Mark A. White

Publikováno v: ResearcherID

For some proteins, dithioation of DNA phosphate is known to enhance binding affinities. For the Antennapedia (Antp) homedomain - DNA complex, we have mechanistically characterized this phenomenon by integrated use of fluorescence, isothermal calorime

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::242333b0217dd9080605b517397d2da5
https://doi.org/10.1016/j.bpj.2015.11.2998

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Characterization of a Human 12/15-Lipoxygenase Promoter Variant Associated with Atherosclerosis Identifies Vimentin as a Promoter Binding Protein

Autor: Kurtis M. Anderson, Myriam Fornage, David H. Hawke, Susmita Samanta, David G. Gorenstein, Sean Moran

Publikováno v: PLoS ONE
PLoS ONE, Vol 7, Iss 8, p e42417 (2012)

Background Sequence variation in the human 12/15 lipoxygenase (ALOX15) has been associated with atherosclerotic disease. We functionally characterized an ALOX15 promoter polymorphism, rs2255888, previously associated with carotid plaque burden. Metho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aeb060e7c1acca7c652238554b28f01
http://europepmc.org/articles/PMC3413658

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NMR Assignments of the Sylvatic Dengue 1 Virus Envelope Protein Domain III

Autor: Li Li, Fiona J. May, David G. Gorenstein, David E. Volk, David W.C. Beasley, Kurtis M. Anderson, Sai Hari A. Gandham, Alan D.T. Barrett

Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289-K400, of the envelope protein from the sylvatic strain (P72-1244) of the dengue 1 virus, containing mutations N336S and E370K, using

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fac77bebde4f159d70e912b3147f4b0
https://europepmc.org/articles/PMC2593834/

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Entropic Enhancement of Protein-DNA Affinity by Oxygen-to-Sulfur Substitution in DNA Phosphate

Autor: Kurtis M. Anderson, David G. Gorenstein, Junji Iwahara, Dan Nguyen, Mark A. White, Levani Zandarashvili

Publikováno v: Biophysical Journal. (5):1026-1037

Dithioation of DNA phosphate is known to enhance binding affinities, at least for some proteins. We mechanistically characterized this phenomenon for the Antennapedia homeodomain-DNA complex by integrated use of fluorescence, isothermal titration cal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb49a8d16a5550076e24c98d45eb8678

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