Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alana K. Simorellis"'
Autor:
Derrick E. Johnson, Johnathan Chittuluru, Quyen Q. Hoang, Jared R. Auclair, Iva Perovic, Alana K. Simorellis, Anuradha Landeru, Shulin Ju, Gregory A. Petsko, Alice Kaganovich, Linh T.T. Nguyen, Dagmar Ringe, ChulHee Kang, Mark R. Cookson, Jeffrey N. Agar, Wei Wang, Francisco J. Asturias, Brian N. Webb, Jingling Liao, Thomas C. Pochapsky
Publikováno v:
Proceedings of the National Academy of Sciences. 108:17797-17802
A heterologously expressed form of the human Parkinson disease-associated protein α-synuclein with a 10-residue N-terminal extension is shown to form a stable tetramer in the absence of lipid bilayers or micelles. Sequential NMR assignments, intramo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db3fbdf2ba8607a0725b42c33cd831bf
https://doi.org/10.1073/pnas.1113260108
https://doi.org/10.1073/pnas.1113260108
Publikováno v:
Biochemistry. 48:4254-4261
The dynamics of any protein, be it structural, regulatory or enzymatic, must be taken into consideration when trying to understand biological function. Metalloproteins provide excellent models for the role of protein dynamics in function, particularl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3695d877ff30b6cbbfd942d515a330f0
https://doi.org/10.1021/bi900002k
https://doi.org/10.1021/bi900002k
Publikováno v:
Journal of the American Chemical Society. 128:5082-5090
The effects of low temperature and ionic strength on water encapsulated within reverse micelles were investigated by solution NMR. Reverse micelles composed of AOT and pentane and solutions with varying concentrations of NaCl were studied at temperat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::895abd29b73e74f0d1eefea1d12aea17
https://doi.org/10.1021/ja0568401
https://doi.org/10.1021/ja0568401
Publikováno v:
Journal of the American Chemical Society. 127:13553-13560
Water-soluble proteins encapsulated within reverse micelles may be studied under a variety of conditions, including low temperature and a wide range of buffer conditions. Direct high-resolution detection of information relating to protein folding int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac295c4537f522251deb09b041e64343
https://doi.org/10.1021/ja052805i
https://doi.org/10.1021/ja052805i
Autor:
Alana K. Simorellis, Thomas C. Pochapsky, Bo OuYang, Kathleen S. Molnar, Yoshitomo Hamuro, Stephen J. Coales
Backbone dynamics of the camphor monoxygenase cytochrome P450(cam) (CYP101) as a function of oxidation/ligation state of the heme iron were investigated via hydrogen/deuterium exchange (H/D exchange) as monitored by mass spectrometry. Main chain amid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d3b358f9901ea178fef5fd25a3a8b13
https://europepmc.org/articles/PMC2279175/
https://europepmc.org/articles/PMC2279175/
Encapsulation of proteins with reverse micelles has recently been identified as an important new biological NMR application. Encapsulation involves transfer of a hydrated protein into the interior chamber formed within an inverted shell of surfactant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b426eadc88c91059631f0ef884c9c657
https://doi.org/10.1016/s0066-4103(07)62004-3
https://doi.org/10.1016/s0066-4103(07)62004-3
Autor:
Peter F. Flynn, Alana K. Simorellis
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 170(2)
Pulsed gradient simulated-echo (PGSE) NMR diffusion measurements provide a facile and accurate means for determining the self-diffusion coefficients for molecules over a wide range of sizes and conditions. The measurement of diffusion in solvents of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a3042156e601b1036f78387e0f0d2fa
https://pubmed.ncbi.nlm.nih.gov/15388096
https://pubmed.ncbi.nlm.nih.gov/15388096
Autor:
Alana K. Simorellis, Peter F. Flynn
Publikováno v:
Journal of the American Chemical Society. 128:9580-9581
Backbone dynamics of ubiquitin confined within AOT reverse micelles have been evaluated based on analysis of 15N NMR relaxation data. Results indicate that upon encapsulation the protein experiences a slight overall increase in the value of the order
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9af9e19cd675bd7a22f71c0efba8b7e
https://doi.org/10.1021/ja061705p
https://doi.org/10.1021/ja061705p
Autor:
Alana K. Simorellis, Shohei Koide, Akihiro Maeno, Kazuyuki Akasaka, Kazumi Hata, Ryo Kitahara, Shigeyuki Yokoyama
Publikováno v:
Biophysical Journal. (4):916-926
Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbe83563a4545722bae5750d26bebc36