The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein

ACS Nano

Volumn 6, Issue 2, 2012, Pages 1332-1346

  Forman, Christopher J ^a   Nickson, Adrian A ^a   Anthony Cahill, Spencer J ^b   Baldwin, Andrew J ^a   Kaggwa, Gillian ^c   Feber, Urs ^c   Sheikh, Khizar ^c   Jarvis, Suzanne P ^c   Barker, Paul D ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b WESTERN WASHINGTON UNIVERSITY   (United States)

^c UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

AFM; amyloid; electron transfer; molecular electronics; self assembly

Indexed keywords

AFM; AFM IMAGING; AMYLOID; AMYLOID FIBERS; COFACTOR BINDING; CYTOCHROME B; ELECTRON TRANSFER; FIBER DESIGN; FIBER GEOMETRIES; FIBER MORPHOLOGY; FIBER STRUCTURES; FUSION PROTEINS; HIGH AFFINITY; SELF ASSEMBLED STRUCTURES; SMALL MOLECULES; UV-VIS SPECTROSCOPY;

CONFORMATIONS; ELECTRON TRANSITIONS; FIBERS; GLYCOPROTEINS; MOLECULAR ELECTRONICS; MORPHOLOGY; PORPHYRINS; ULTRAVIOLET SPECTROSCOPY; ULTRAVIOLET VISIBLE SPECTROSCOPY;

PROTEINS;

AMYLOID; CYTOCHROME B; HEME; HYBRID PROTEIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON TRANSPORT; METABOLISM; PROTEIN MULTIMERIZATION; SRC HOMOLOGY DOMAIN;

AMYLOID; CYTOCHROME B GROUP; ELECTRON TRANSPORT; HEME; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 84857776493     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn204140a     Document Type: Article

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