About: Catalytic Unfolding and Proteolysis of Cytochrome c Inducedby Synthetic Binding Agents

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Attributs	Valeurs
type	work Article
Is Part Of	http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/w
Subject	Article
Title	Catalytic Unfolding and Proteolysis of Cytochrome c Inducedby Synthetic Binding Agents
has manifestation of work	http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/m/print http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/m/web
related by	http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/authorship/1 http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/authorship/2 http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/authorship/3
Author	Groves Kevin Hamilton Andrew Wilson Andrew J.
Abstract	A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibilityof cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. Thefree energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol inthe bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalentof metalloporphyrin to effect complete, rapid digestion in the presence of a protease.1
article type	research-article
is part of this journal	Journal of the American Chemical Society

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