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Article(9)
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Archives of Biochemistry and Biophysics(3)
Biochimica et Biophysica Acta - Proteins and Proteomics(1)
Biochimie(1)
Biomolecules(1)
Journal of Biochemistry(1)
Binding of glucose to the D-galactose/D-glucose-binding protein from Escherichia coli restores the native protein secondary structure and thermostability that are lost upon calcium depletion
ArticleAbstract: The effect of the depletion of calcium on the structure and thermal stability of the D-galactose/D-gPalabras claves:Galactose/glucose-binding protein, Infrared spectroscopy, Protein stability, Protein structureAutores:Alessio Ausili, Bertoli E., D’auria S., Marabotti A., Rossi M., Scognamiglio V., Staiano M., Tanfani F., Varriale A.Fuentes:googlescopusA spectroscopic study on secondary structure and thermal unfolding of the plant toxin gelonin confirms some typical structural characteristics and unravels the sequence of thermal unfolding events
ArticleAbstract: Gelonin from the Indian plant Gelonium multiflorum belongs to the type I ribosome-inactivating protePalabras claves:Gelonin, Immunotoxins, Infrared spectroscopy, Ribosome-inactivating protein, Thermal unfolding, Two-dimensional correlation spectroscopyAutores:Alessio Ausili, Scirè A., Tanfani F.Fuentes:googlescopusDespite their structural similarities, the cytosolic isoforms of human Hsp90 show different behaviour in thermal unfolding due to their conformation: An FTIR study
ArticleAbstract: Heat shock proteins 90 (Hsp90) are chaperones that promote the proper folding of other proteins undePalabras claves:Human Hsp90, Infrared spectroscopy, Protein structure, Thermal stability, UnfoldingAutores:Alessio AusiliFuentes:googlescopusStructural basis of the destabilization produced by an amino-terminal tag in the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus
ArticleAbstract: We have previously shown that the major ion-pairs network of the tetrameric β-glycosidase from the hPalabras claves:Archaea, Glycoside hydrolase, Infrared spectroscopy, Quaternary structure, Thermal stabilityAutores:Alessio Ausili, Cobucci-Ponzano B., D'Avino R., Di Lauro B., Moracci M., Rossi M., Scirè A., Tanfani F.Fuentes:googlescopusStudies on the interaction of alyteserin 1c peptideand its cationic analogue with model membranes imitating mammalian and bacterial membranes
ArticleAbstract: Antimicrobial peptides (AMPs) are effector molecules of the innate immune system and have been isolaPalabras claves:Alyteserin 1c, calorimetry, Infrared spectroscopy, Model membranes, molecular dynamics, referencesAutores:Alessio Ausili, Aragón-Muriel A., Mosquera J.L., Oñate-Garzón J., Polo-Cerón D., Rojasa O.E., Sánchez K.Fuentes:googlescopusThe binding of different model membranes with PKCε C2 domain is not dependent on membrane curvature but affects the sequence of events during unfolding
ArticleAbstract: The C2 domain of novel protein kinases C (nPKC) binds to membranes in a Ca2+-independent way contribPalabras claves:Infrared spectroscopy, Membrane curvature, Model membranes, Protein kinase Cε, Protein unfoldingAutores:Alessio Ausili, Corbalán-García S., Gómez‐Fernández J.C.Fuentes:googlescopusThe increase in positively charged residues in cecropin D-like Galleria mellonella favors its interaction with membrane models that imitate bacterial membranes
ArticleAbstract: A comparative study of three synthetic peptides, namely neutral Cecropin D-like G. mellonella (WT) aPalabras claves:Antimicrobial peptide, calorimetry, Cationic charge, Galleria mellonella, Infrared spectroscopy, Peptide-membrane interactionsAutores:Alessio Ausili, Aranda F.J., Gómez‐Fernández J.C., Manrique-Moreno M., Oñate-Garzón J., Patiño E., Torrecillas A.Fuentes:googlescopusThe interaction of the Bax C-terminal domain with negatively charged lipids modifies the secondary structure and changes its way of insertion into membranes
ArticleAbstract: Fourier transform infrared spectroscopy (FTIR) was used to study the secondary structure of peptidesPalabras claves:apoptosis, ATR-FTIR, BAX, Infrared spectroscopyAutores:Alessio Ausili, Corbalán-García S., Gómez‐Fernández J.C., Martínez-Senac M., Torrecillas A.Fuentes:googlescopusThe thermal unfolding of the ribosome-inactivating protein saporin-S6 characterized by infrared spectroscopy
ArticleAbstract: Abstract Saporin-S6 is a plant toxin belonging to the type 1 ribosome-inactivating protein (RIP) famPalabras claves:Infrared spectroscopy, Ribosome-inactivating protein, Saporin-S6, Thermal unfoldingAutores:A Ausili, A Scir�, Alessio Ausili, F. Tanfani, M. Sánchez, Sánchez M., Scirè A., Tanfani F.Fuentes:googlerraaescopus