Zobrazeno 1 - 8
of 8
pro vyhledávání: '"J. Ricardo Alcala"'
Publikováno v:
Brain Research. 693:179-186
Light transmittance (T) in the CA1 region of hippocampal slices was measured during exposure to media of various osmolarities to determine the utility of optical measurements as an index of changes in cell volume. In slices positioned at the gas-liqu
Autor:
J. Ricardo Alcala
Publikováno v:
The Journal of Chemical Physics. 101:4578-4584
Proteins change their structure constantly due to their conformational flexibility and dynamic nature. The structure of the molecule follows a trajectory in conformational space determined by the hierarchy of conformational substates of the protein.
Publikováno v:
Review of Scientific Instruments. 64:1554-1560
An instrument to measure the excited‐state lifetimes of phosphorescent materials in real time is described. This apparatus uses pulsed and frequency‐doubled Nd:YAG solid‐state laser for excitation, sampler for data acquisition, and frequency do
Autor:
J. Ricardo Alcala
Publikováno v:
Topics in Fluorescence Spectroscopy ISBN: 0306447843
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0050d8a3e657a825cc3d4fa56d1ba5b
https://doi.org/10.1007/0-306-47060-8_9
https://doi.org/10.1007/0-306-47060-8_9
Autor:
J. Ricardo Alcala
Publikováno v:
Review of Scientific Instruments. 62:1672-1673
Publikováno v:
Alcala, JR; Gratton, E; & Jameson, DM. (1985). A multifrequency phase fluorometer using the harmonic content of a mode-locked laser. Analytical Instrumentation, 14(3-4), 225-250. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3mf1q4fd
We describe the construction and operation of a cross-correlation phase and modulation fluorometer which uses the harmonic content of a high repetition rate mode-locked laser as the excitation source. A mode-locked argon ion laser is used to synchron
Publikováno v:
Structure and Dynamics of Nucleic Acids, Proteins, and Membranes ISBN: 9781468453102
Proteins are flexible structures; their flexibility is crucial for biological function. The physical origin of protein flexibility has been discussed and it arises from the intrinsic flexibility of the polypeptide chain.1,2 The time scale of protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12de480bb10f58f15e563d80a1a0a14e
https://doi.org/10.1007/978-1-4684-5308-9_11
https://doi.org/10.1007/978-1-4684-5308-9_11
Publikováno v:
Fluorescent Biomolecules ISBN: 9781468456219
It is now well established that proteins in their native conformation can exist in a large number of subconformations slightly different one from the other (Lakowicz & Weber, 1973; Austin et al., 1975; Careri et al., 1975, 1979; Karplus & McCammon, 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55967436fbd19108af42a0053663212c
https://doi.org/10.1007/978-1-4684-5619-6_2
https://doi.org/10.1007/978-1-4684-5619-6_2