Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Tiandi Zhuang"'
Autor:
Tiandi Zhuang, Lukas K. Tamm
Publikováno v:
Angewandte Chemie International Edition. 53:5897-5902
Protein nanopores have attracted much interest for nucleic acid sequencing, chemical sensing, and protein folding at the single molecule level. The outer membrane protein OmpG from E. coli stands out because it forms a nanopore from a single polypept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e6e90272140773b8cf8b8a09bdeaac4
https://doi.org/10.1002/anie.201400400
https://doi.org/10.1002/anie.201400400
Publikováno v:
Journal of the American Chemical Society. 135:15101-15113
The outer membrane protein G (OmpG) is a monomeric 33 kDa 14-stranded β-barrel membrane protein functioning as a nonspecific porin for the uptake of oligosaccharides in Escherichia coli. Two different crystal structures of OmpG obtained at different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bd7b3d3a7aa4173e469a5c2a100b583
https://doi.org/10.1021/ja408206e
https://doi.org/10.1021/ja408206e
Autor:
Frank D. Sönnichsen, Wade D. Van Horn, Paul J. Barrett, Tiandi Zhuang, Dungeng Peng, Ji-Hun Kim, Zhenwei Lu, Charles R. Sanders, Sijo Mathew, Jiang Chen, Min-Kyu Cho, Yuanli Song
Publikováno v:
Biochemistry. 52:1303-1320
From roughly 1985 through the start of the new millennium, the cutting edge of solution protein nuclear magnetic resonance (NMR) spectroscopy was to a significant extent driven by the aspiration to determine structures. Here we survey recent advances
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f4c5fe495531a66bf3fd57e804a54f2
https://doi.org/10.1021/bi4000436
https://doi.org/10.1021/bi4000436
Autor:
Charles R. Sanders, Min-Kyu Cho, Qiuyan Chen, Vsevolod V. Gurevich, Tiandi Zhuang, Tina M. Iverson, Sergey A. Vishnivetskiy
Publikováno v:
Proceedings of the National Academy of Sciences. 110:942-947
Solution NMR spectroscopy of labeled arrestin-1 was used to explore its interactions with dark-state phosphorylated rhodopsin (P-Rh), phosphorylated opsin (P-opsin), unphosphorylated light-activated rhodopsin (Rh*), and phosphorylated light-activated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc8a773852e254c68d58fcae4e73f9d8
https://doi.org/10.1073/pnas.1215176110
https://doi.org/10.1073/pnas.1215176110
Solution NMR Approaches for Establishing Specificity of Weak Heterodimerization of Membrane Proteins
Publikováno v:
Journal of the American Chemical Society. 133:20571-20580
Solution NMR provides a powerful approach for detecting complex formation involving weak to moderate intermolecular affinity. However, solution NMR has only rarely been used to detect complex formation between two membrane proteins in model membranes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4754878221c020dd3f0a1f0874739d0e
https://doi.org/10.1021/ja208972h
https://doi.org/10.1021/ja208972h
Publikováno v:
Biochemistry. 49:10473-10485
Arrestins specifically bind activated and phosphorylated G protein-coupled receptors and orchestrate both receptor trafficking and channel signaling through G protein-independent pathways via direct interactions with numerous nonreceptor partners. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::127825dd9227bf96e7fd75a75b86cd6f
https://doi.org/10.1021/bi101596g
https://doi.org/10.1021/bi101596g
Autor:
Caroline M. Watson, Joshua S. Sharp, Ireneusz Janik, Robert J. Woods, Tiandi Zhuang, Olga Charvátová
Publikováno v:
Analytical Chemistry. 81:2496-2505
Hydroxyl radical footprinting is a valuable technique for studying protein structure, but care must be taken to ensure that the protein does not unfold during the labeling process due to oxidative damage. Footprinting methods based on submicrosecond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d93eb85148faaa087abec484c228304c
https://doi.org/10.1021/ac802252y
https://doi.org/10.1021/ac802252y
Publikováno v:
Protein Science. 17:1220-1231
The determination of the location and conformation of a natural ligand bound to a protein receptor is often a first step in the rational design of molecules that can modulate receptor function. NMR observables, including NOEs, often provide the basis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08afdc24c62a78f6485f77003c1269d0
https://doi.org/10.1110/ps.034561.108
https://doi.org/10.1110/ps.034561.108
Publikováno v:
Journal of the American Chemical Society. 129:4834-4839
The study of bound-state conformations of ligands interacting with proteins is important to the understanding of protein function and the design of drugs that alter function. Traditionally, transferred nuclear Overhauser effects (trNOEs), measured fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df8c39ee8afb636977e321b2ace193fb
https://doi.org/10.1021/ja069145h
https://doi.org/10.1021/ja069145h
Autor:
Vsevolod V. Gurevich, Sergey A. Vishnivetskiy, Qiuyan Chen, Tina M. Iverson, Tarjani M. Thaker, Min-Kyu Cho, Tiandi Zhuang, Charles R. Sanders
Publikováno v:
Methods in Molecular Biology ISBN: 9781493923298
G-protein-coupled receptors (GPCRs) are essential mediators of information transfer in eukaryotic cells. Interactions between GPCRs and their binding partners modulate the signaling process. For example, the interaction between GPCR and cognate G pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c50208e8221eb67176fe9c5cd68c5bb
https://europepmc.org/articles/PMC4520306/
https://europepmc.org/articles/PMC4520306/
