Výsledky vyhledávání - "Spadaccini, R."

NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping

Autor: Spadaccini, R., Ercole, C., Gentile, M.A., Sanfelice, D., Boelens, R., Wechselberger, R.W., Batta, G., Bernini, A., Niccolai, N., Picone, D., NMR Spectroscopy, Sub NMR Spectroscopy

Publikováno v: PLoS ONE
PLoS One, 7(1), 1. Public Library of Science
PLoS ONE, Vol 7, Iss 1, p e29076 (2012)

Three-dimensional domain swapping is a common phenomenon in pancreatic-like ribonucleases. In the aggregated state, these proteins acquire new biological functions, including selective cytotoxicity against tumour cells. RNase A is able to dislocate b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50c581a1dca2f23e452572545e6f95ee
http://hdl.handle.net/11365/21145

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Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin

Autor: SPADACCINI R., CRESCENZI O., TANCREDI T., DE CASAMASSIMI N., SAVIANO G., SCOGNAMIGLIO R., DI DONATO, ALBERTO, TEMUSSI, PIERO ANDREA

Publikováno v: Journal of Molecular Biology 305 (2001): 505–514.
info:cnr-pdr/source/autori:R. Spadaccini, O. Crescenzi, T. Tancredi, N. De Casamassimi, G. Saviano, R. Scognamiglio, A. Di Donato and P.A. Temussi/titolo:Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin/doi:/rivista:Journal of Molecular Biology/anno:2001/pagina_da:505/pagina_a:514/intervallo_pagine:505–514/volume:305

The sweet protein MNEI is a construct of 96 amino acid residues engineered by linking, with a Gly-Phe dipeptide, chains B and A of monellin, a sweet protein isolated from Discoreophyllum cuminsii. Here, the solution structure of MNEI was determined o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::be3153c5b3b6329cc917987be8e6f8ad
http://hdl.handle.net/11588/136595

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