Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Shane Price"'
Autor:
Eduardo González Cabañes, Penelope L. Kuhn, Sara Ortega-Merino, Ana M. Ullán de la Fuente, Lawrence Herringer, Shane Price, Carla Saldaña, Lucy Madden, Anna Bartel, Estela Rojo-Hernández
Publikováno v:
Psychology, Society & Education, Vol 14, Iss 2 (2022)
This study explored the practice and spacing-of-practice effects in people living with dementia during an artistic painting activity. The video recordings of 23 participants were systematically observed during their first and fourth session of the ac
Externí odkaz:
https://doaj.org/article/9653af9c34524b3e8929bc0c40429eb6
Publikováno v:
The Journal of Physical Chemistry B. 114:5895-5902
Fluorescence correlation spectroscopy (FCS) is a robust method for the detection of intramolecular dynamics in proteins but is also susceptible to interference from other dynamic processes such as triplet kinetics and photobleaching. We describe an a
Autor:
Jay R. Unruh, E. Shane Price, Carey K. Johnson, Brian D. Slaughter, Ramona J. Bieber Urbauer, Jason L. Huynh
Publikováno v:
Journal of the American Chemical Society. 127:12107-12114
We used single-pair fluorescence resonance energy transfer (spFRET) measurements to characterize denatured and partially denatured states of the multidomain calcium signaling protein calmodulin (CaM) in both its apo and Ca(2+)-bound forms. The result
Publikováno v:
Journal of Engineering Materials and Technology. 126:360-367
Commercial methods for the mechanical design of part and die shapes often rely on trial-and-error methods applied to either experiments or simulation, as guided by intuition. Academic alternatives based on optimization techniques have had slow accept
Fluorescence correlation spectroscopy (FCS) can be coupled with Forster resonance energy transfer (FRET) to detect intramolecular dynamics of proteins on the microsecond time scale. Here we describe application of FRET-FCS to detect fluctuations with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04a7927c6feea2ce7ab35efbb8a925eb
https://europepmc.org/articles/PMC3151148/
https://europepmc.org/articles/PMC3151148/
Publikováno v:
The Journal of chemical physics. 134(14)
We introduce a new approach to analyze single-molecule Forster resonance energy transfer (FRET) data. The method recognizes that FRET efficiencies assumed by traditional ensemble methods are unobservable for single molecules. We propose instead a met
Publikováno v:
Biophysical Journal. 98(3)
Measurements of the distance between two dye molecules covalently linked to the calcium signaling protein calmodulin (CaM) have been previously performed by our group to investigate the conformations of CaM in solution. It was shown that calmodulin e
A voltage-controlled birefringent cell based on ceramic PMN-PT material is used to enable fast intensity modulation of femtosecond laser pulses in the 800 nm wavelength window. The birefringent cell based on a PMN-PT compound has comparatively high e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2159cb763975bb2b0c210529253bd005
https://europepmc.org/articles/PMC2678787/
https://europepmc.org/articles/PMC2678787/
Autor:
Steven M. Bishop, E. Shane Price, Sangeeta B. Joshi, C. Russell Middaugh, Cynthia N. Oliver, Joshua D. Ramsey, Michelle L. Gill, Tim J. Kamerzell
Publikováno v:
Journal of pharmaceutical sciences. 98(7)
Understanding the relationship between protein dynamics and stability is of paramount importance to the fields of biology and pharmaceutics. Clarifying this relationship is complicated by the large amount of experimental data that must be generated a
Publikováno v:
Reviews in Fluorescence 2006 ISBN: 9780387293424
The results described here demonstrate that single-molecule fluorescence spectroscopy of molecules freely diffusing in solution can yield unique information about both the dynamics and conformations of proteins. We used single-molecule FRET to detect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36dc069389a6622f46ff86f3d58f558e
https://doi.org/10.1007/0-387-33016-x_11
https://doi.org/10.1007/0-387-33016-x_11