Show simple item record Korendovych, IV Senes, A Kim, YH Lear, JD Fry, HC Therien, MJ Blasie, JK Walker, FA Degrado, WF
dc.coverage.spatial United States 2011-06-21T17:26:23Z 2010-11-10
dc.identifier.citation J Am Chem Soc, 2010, 132 (44), pp. 15516 - 15518
dc.description.abstract The de novo design of membrane proteins remains difficult despite recent advances in understanding the factors that drive membrane protein folding and association. We have designed a membrane protein PRIME (PoRphyrins In MEmbrane) that positions two non-natural iron diphenylporphyrins (Fe(III)DPP's) sufficiently close to provide a multicentered pathway for transmembrane electron transfer. Computational methods previously used for the design of multiporphyrin water-soluble helical proteins were extended to this membrane target. Four helices were arranged in a D(2)-symmetrical bundle to bind two Fe(II/III) diphenylporphyrins in a bis-His geometry further stabilized by second-shell hydrogen bonds. UV-vis absorbance, CD spectroscopy, analytical ultracentrifugation, redox potentiometry, and EPR demonstrate that PRIME binds the cofactor with high affinity and specificity in the expected geometry.
dc.format.extent 15516 - 15518
dc.language eng
dc.language.iso en_US en_US
dc.relation.ispartof J Am Chem Soc
dc.relation.isversionof 10.1021/ja107487b
dc.subject Circular Dichroism
dc.subject Membrane Proteins
dc.subject Models, Molecular
dc.subject Multiprotein Complexes
dc.subject Porphyrins
dc.subject Protein Binding
dc.subject Protein Folding
dc.title De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US 2010-11-10 en_US
duke.description.endpage 15518 en_US
duke.description.issue 44 en_US
duke.description.startpage 15516 en_US
duke.description.volume 132 en_US
dc.relation.journal Journal of the American Chemical Society en_US
pubs.issue 44
pubs.organisational-group /Duke
pubs.organisational-group /Duke/Pratt School of Engineering
pubs.organisational-group /Duke/Pratt School of Engineering/Biomedical Engineering
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Chemistry
pubs.publication-status Published
pubs.volume 132
dc.identifier.eissn 1520-5126

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