Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Eugenio Vitrano"'
Publikováno v:
The Journal of Physical Chemistry B. 113:9606-9613
In this work we report the results of a broadband dielectric spectroscopy study on the dynamics of a globular protein, myoglobin, in confined geometry, i.e. encapsulated in a porous silica matrix, at low hydration levels, where about only one or two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c33944643be3067a1b1c4aaeba257e59
https://doi.org/10.1021/jp901420r
https://doi.org/10.1021/jp901420r
Autor:
Peter Galajda, Eugenio Vitrano, Alexandra Gassmann, Lorenzo Cordone, Andreas Ostermann, Fritz G. Parak
Publikováno v:
European Biophysics Journal. 27:173-176
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07dac4b92d01b962c240c78931148c4e
https://doi.org/10.1007/s002490050123
https://doi.org/10.1007/s002490050123
Publikováno v:
Biophysical Journal. 73(2):959-965
We have studied the local dynamics of calf thymus double-helical DNA by means of an "optical labeling" technique. The study has been performed by measuring the visible absorption band of the cationic dye ethidium bromide, both free in solution and bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7022de5ffe451074c51852794c936719
We report a study on the thermal behaviour of the infrared Water Association Band (WAB) in dry binary saccharide–water systems (containing trehalose, sucrose, maltose, and raffinose). This is a follow-up of preceding studies on analogous carboxymyo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cd6562c077f496b502bb044bcfb998f
http://hdl.handle.net/10447/53931
http://hdl.handle.net/10447/53931
Autor:
W. Yu, Lorenzo Cordone, Maurizio Leone, E. E. Di Iorio, Eugenio Vitrano, Antonio Cupane, U.R. Hiltpold, K.H. Winterhalter
Publikováno v:
Scopus-Elsevier
In this work we report the thermal behavior (10–300 K) of the Soret band lineshape of deoxy and carbonmonoxy derivatives of Asian elephant (Elephas maximus) and horse myoglobins together with their carbon monoxide recombination kinetics after flash
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da944eaf37b764549c72b8d804680d3e
Publikováno v:
Biophysical Chemistry. 39:161-169
We have studied the effects of organic cosolvents (monohydric alcohols and formamide) on the oxygen affinity of human fetal hemoglobin stripped of phosphates and have compared them with the effects of the same cosolvents on the oxygen affinity of hum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea2679978bdd9718f03e140a6e61aa3b
https://doi.org/10.1016/0301-4622(91)85018-l
https://doi.org/10.1016/0301-4622(91)85018-l
Publikováno v:
Biophysical Chemistry. 38:213-224
We have measured the optical absorption spectra of azurin and stellacyanin in the wavelength range 1100-350 nm and in the temperature interval 290–20 K. Samples are protein aqueous solutions containing 65% (v/v) glycerol or ethylene glycol as cryop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d26f09ee0e74a14412183d756c4894d
https://doi.org/10.1016/0301-4622(90)87003-4
https://doi.org/10.1016/0301-4622(90)87003-4
Publikováno v:
Biophysical Chemistry. 37:171-181
We report on oxygen binding to partially oxidized (aquomet) hemoglobin. The fractional saturation with oxygen is evaluated by deconvoluting the optical absorption spectra, in the 500–700 nm wavelength region, in terms of oxyhemoglobin, deoxyhemoglo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59105d4f14590cfbc92692a3447e5812
https://doi.org/10.1016/0301-4622(90)88017-m
https://doi.org/10.1016/0301-4622(90)88017-m
Publikováno v:
Biopolymers. 29:639-643
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9e48d2648bad78f7b37159668a08b91
https://doi.org/10.1002/bip.360290316
https://doi.org/10.1002/bip.360290316
Autor:
Maurizio Leone, Antonio Cupane, Fritz G. Parak, Eugenio Vitrano, Niklas Engler, Lorenzo Cordone, Marco Cammarata
Publikováno v:
European biophysics journal : EBJ. 34(7)
In this work the temperature dependence of the Soret band line shape in carbon-monoxy myoglobin is re-analyzed by using both the full correlator approach in the time domain and the frequency domain approach. The new analyses exploit the full density
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0969910dc7cdbbb7490444e766320138
https://pubmed.ncbi.nlm.nih.gov/16215751
https://pubmed.ncbi.nlm.nih.gov/16215751