Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Ciara Kyne"'
Autor:
Ciara Kyne, Peter B. Crowley
Publikováno v:
Biochemistry. 56:5026-5032
Although essential to numerous biotech applications, knowledge of molecular recognition by arginine-rich motifs in live cells remains limited. 1H,15N HSQC and 19F NMR spectroscopies were used to investigate the effects of C-terminal −GRn (n = 1–5
Publikováno v:
Protein Science. 26:258-267
Decades of dilute-solution studies have revealed the influence of charged residues on protein stability, solubility and stickiness. Similar characterizations are now required in physiological solutions to understand the effect of charge on protein be
Autor:
Peter B. Crowley, Ciara Kyne
Publikováno v:
The FEBS Journal. 283:3016-3028
Current models of the cell interior emphasise its crowded, chemically complex and dynamically organised structure. Although the chemical composition of cells is known, the cooperative intermolecular interactions that govern cell ultrastructure are po
Publikováno v:
Protein Science. 24:310-318
Protein characterization in situ remains a major challenge for protein science. Here, the interactions of ΔTat-GB1 in Escherichia coli cell extracts were investigated by NMR spectroscopy and size exclusion chromatography (SEC). ΔTat-GB1 was found t
Autor:
Christoph Wettstein, Fred Lisdat, Ciara Kyne, Helmuth Möhwald, Peter B. Crowley, Aishling M. Doolan
Publikováno v:
Nanoscale. 6(22)
Artificial assemblies consisting of the cationic cytochrome c (cyt c) and double-stranded DNA are interesting for the field of biohybrid systems because of the high electro-activity of the incorporated redox protein. However, little is known about th
Autor:
Lila M. Gierasch, Andres Binolfi, Peter B. Crowley, Francois Xavier Theillet, Anne Gershenson, Tamara Frembgen-Kesner, Gary J. Pielak, Adrian H. Elcock, Karan S. Hingorani, Philipp Selenko, Conggang Li, Mohona Sarkar, Ciara Kyne
Publikováno v:
Chemical Reviews
Chemical reviews, 114(13): 6661–6714
Chemical reviews, 114(13): 6661–6714
It has long been axiomatic that a protein’s structure determines its function. Intrinsically disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure–function paradigm. They do not exhibit stable secondary and/or terti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bbdcaaf7f55f0577c1593d21b7b069e
http://hdl.handle.net/10379/14144
http://hdl.handle.net/10379/14144
Publikováno v:
Chemical communications (Cambridge, England). 48(86)
Fluorine-containing amino acids are valuable probes for the biophysical characterization of proteins. Current methods for (19)F-labeled protein production involve time-consuming genetic manipulation, compromised expression systems and expensive reage