Výsledky vyhledávání - "protein-inhibitor interaction"

Surface Plasmon Resonance: A Useful Strategy for the Identification of Small Molecule Argonaute 2 Protein Binders

Autor: Francesco Fazi, Gianni Colotti, Elena Poser, Ilaria Genovese, Teresa Bellissimo, Silvia Masciarelli

Publikováno v: pp. 223–237. New York: Springer, 2017
info:cnr-pdr/source/autori:Poser, Elena; Genovese, Ilaria; Masciarelli, Silvia; Bellissimo, Teresa; Fazi, Francesco; Colotti, Gianni/titolo:Surface Plasmon Resonance: A Useful Strategy for the Identification of Small Molecule Argonaute 2 Protein Binders./titolo_volume:/curatori_volume:/editore: /anno:2017
Methods in Molecular Biology ISBN: 9781493965618

Surface plasmon resonance (SPR) is one of the most important techniques for the detection and the characterization of molecular interactions. SPR technology is a label-free approach for monitoring biomolecular interactions in real time. The binding o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dd46aa141d722239284beb737a66989
https://publications.cnr.it/doc/370232

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Influence of pH on the Structure and Function of Kiwi Pectin Methylesterase Inhibitor

Autor: Alfonso Giovane, Rossana D'Avino, Alessandro Bonavita, Maria Antonietta Ciardiello, Luigi Servillo, Vitale Carratore

Publikováno v: Journal of agricultural and food chemistry (2016). doi:10.1021/acs.jafc.6b01718
info:cnr-pdr/source/autori:Alessandro Bonavita, Vitale Carratore, Maria Antonietta Ciardiello, Alfonso Giovane, Luigi Servillo, and Rossana D'Avino/titolo:Influence of pH on the Structure and Function of Kiwi Pectin Methylesterase Inhibitor/doi:10.1021%2Facs.jafc.6b01718/rivista:Journal of agricultural and food chemistry/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume

Pectin methylesterase is a pectin modifying enzyme that plays a key role in plant physiology. It is also an important quality-related enzyme in plant-based food products. The pectin methylesterase inhibitor (PMEI) from kiwifruit inhibits this enzyme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80c7f141ffe4c74fe3009aa80611b09e
https://pubmed.ncbi.nlm.nih.gov/27335009

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Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor

Autor: Laura Camardella, Lisa Tuppo, Alfonso Giovane, Vito Carratore, M. Antonietta Ciardiello, Maurizio Tamburrini, Benedetta Mattei

Publikováno v: Journal of agricultural and food chemistry 52 (2004): 7700–7703. doi:10.1021/jf0491963
info:cnr-pdr/source/autori:Ciardiello M.A.; Tamburrini M.; Tuppo L.; Carratore V.; Giovane A.; Mattei B.; Camardella L./titolo:Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor/doi:10.1021%2Fjf0491963/rivista:Journal of agricultural and food chemistry/anno:2004/pagina_da:7700/pagina_a:7703/intervallo_pagine:7700–7703/volume:52

Pectin methylesterase was purified from kiwi (Actinidia chinensis) and kaki fruit ( Diospyros kaki). The pH values of the fruit homogenates were 3.5 and 6.2, respectively. The kiwi enzyme is localized in the cell wall and has a neutral-alkaline pI, w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::828da0ac1df0b60558cccc70e229a050

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