Výsledky vyhledávání - "Ettore Bismuto"

Molecular dynamics simulation of the acidic compact state of apomyoglobin from yellowfin tuna

Autor: G. Ulrich Nienhaus, Martin Sikor, Don C. Lamb, Emiddio Di Maggio, Ettore Bismuto, Stefan Pleus, Carlheinz Röcker

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 74:273-290

A molecular model of the acidic compact state of apomyoglobin (A-state) from yellowfin tuna was obtained using molecular dynamics simulations (MD) by calculating multiple trajectories. To cause partial unfolding within a reasonable amount of CPU time

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a84592b113e08e95d11f4b26aad3946
https://doi.org/10.1002/prot.22149

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Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi-chaperone complex in human epidermoid cancer cells

Autor: Alberto Abbruzzese, Fabrizio Mancinelli, Monica Marra, Michele Caraglia, Rita Massa, Alfredo Budillon, Ettore Bismuto, G. d'Ambrosio, Antonio Giordano

Publikováno v: Università degli Studi di Siena-IRIS

The exposure to non-thermal microwave electromagnetic field (MW-EMF) at 1.95 MHz, a frequency used in mobile communication, affects the refolding kinetics of eukaryotic proteins (Mancinelli et al., 2004). On these basis we have evaluated the in vivo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0529b5676ef5b0ffd0661b49bdfad6f5
https://doi.org/10.1002/jcp.20327

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Effects induced by mono- and divalent cations on protein regions responsible for thermal adaptation in �-glycosidase from Sulfolobus solfataricus

Autor: Fabrizio Gentile, Enrico Bertoli, Pietro Amodeo, Andrea Scirè, Roberto Nucci, Ferdinando Febbraio, Fabio Tanfani, Ettore Bismuto, Raffaella Briante

Publikováno v: European Biophysics Journal. 33:38-49

The perturbation induced by mono- and divalent cations on the thermophilicity and thermostability of Solfolobus solfataricus beta-glycosidase, a hyperthermophilic tetrameric enzyme, has been investigated by spectroscopic and computational simulation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98dac32beea017e8a4019f73e7c0a929
https://doi.org/10.1007/s00249-003-0350-7

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Dynamic fluorescence studies of β-glycosidase mutants fromSulfolobus solfataricus: Effects of single mutations on protein thermostability

Autor: Roberto Nucci, Ettore Bismuto, Raffaella Briante, Ferdinando Febbraio, Simona Limongelli

Publikováno v: Proteins: Structure, Function, and Genetics. 51:10-20

Multiple sequence alignment on 73 proteins belonging to glycosyl hydrolase family 1 reveals the occurrence of a segment (83–124) in the enzyme sequences from hyperthermophilic archaea bacteria, which is absent in all the mesophilic members of the f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd50fb6cae6be7a7057dbe3b6b2b0f83
https://doi.org/10.1002/prot.10317

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Dynamics of ANS Binding to Tuna Apomyoglobin Measured with Fluorescence Correlation Spectroscopy

Autor: Enrico Gratton, Ettore Bismuto, Don C. Lamb

Publikováno v: Bismuto, E; Gratton, E; & Lamb, DC. (2001). Dynamics of ANS binding to tuna apomyoglobin measured with fluorescence correlation spectroscopy. Biophysical Journal, 81(6), 3510-3521. doi: 10.1016/S0006-3495(01)75982-6. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/2zd2r3jr

The dynamics of the binding reaction of ANS to native and partly folded (molten globule) tuna and horse apomyoglobins has been investigated by fluorescence correlation spectroscopy and frequency domain fluorometry. The reaction rate has been measured

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32fa538592be3fd6a39b822993acebbd
https://doi.org/10.1016/s0006-3495(01)75982-6

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Structural and dynamic aspects of ?-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies

Autor: Ettore Bismuto, Gaetano Irace, Roberto Nucci, Mosè Rossi

Publikováno v: Proteins: Structure, Function, and Genetics. 35:163-172

The tryptophanyl emission decay of b-glycosidase from the extremophilic archaeon Sulfolobus solfataricus (Sbgly) has been investi- gated by frequency domain fluorometry. The data were analyzed in terms of sum of discrete lifetimes as well as in terms

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6fb364a53115a723676665c2f09c826b
https://doi.org/10.1002/(sici)1097-0134(19990501)35:2<163::aid-prot3>3.0.co

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Perturbation of conformational dynamics, enzymatic activity, and thermostability of β-glycosidase from archaeonSulfolobus solfataricus by pH and sodium dodecyl sulfate detergent

Autor: Roberto Nucci, Gaetano Irace, Sabato D'Auria, Mosè Rossi, Ettore Bismuto

Publikováno v: Proteins: Structure, Function, and Genetics. 27:71-79

The conformational dynamics of β-glycosidase from Sulfolobus solfataricus was investigated by following the emission decay arising from the large number of tryptophanyl residues that are homogeneously dispersed in the primary structure. The fluoresc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::28b69736423fd5f89af6fc6ff6b590ee
https://doi.org/10.1002/(sici)1097-0134(199701)27:1<71::aid-prot8>3.0.co

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Pressure-induced perturbation of ANS-apomyoglobin complex: Frequency domain fluorescence studies on native and acidic compact states

Autor: Enrico Gratton, Ettore Bismuto, Ivana Sirangelo, Gaetano Irace

Publikováno v: Protein Science. 5:121-126

The pressure dependence of the flexibility of the 8-anilino-1-naphthalene sulfonate (ANS)-apomyoglobin complex was investigated in the range between atmospheric pressure and 2.4 kbar by frequency domain fluorometry. We examined two structural states:

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ef046ae97812e8ca608065ce41ef26fa
https://doi.org/10.1002/pro.5560050115

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Unfolding Pathway of Apomyoglobin

Autor: Ettore Bismuto, Gaetano Irace

Publikováno v: Journal of Molecular Biology. 241:103-109

The dynamic properties of the conformational states co-existing during the acid-induced unfolding of tuna apomyoglobin, a single tryptophan-containing protein, have been investigated simultaneously by frequency domain fluorometry. In the transition r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ed39e583ab30d673a431f8603cfd04e
https://doi.org/10.1006/jmbi.1994.1477

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