Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles

Biomaterials

Volumn 33, Issue 22, 2012, Pages 5628-5637

  Parent, Kristin N ^a   Deedas, Christina T ^a   Egelman, Edward H ^b   Casjens, Sherwood R ^c   Baker, Timothy S ^a,d   Teschke, Carolyn M ^a,e  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

^c UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^e UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

Bacteriophage P22; Decoration proteins; Electron cryo microscopy; Helical nanotubes; Three dimensional reconstruction; Viral nanoparticles

Indexed keywords

AFFINITY TAGS; AMINO ACID SUBSTITUTION; CLOSE PROXIMITY; COAT PROTEINS; CRYO-ELECTRON MICROSCOPY; FLUORESCENCE ANISOTROPY; HELICAL COMPLEXES; NANO SCALE; NANOSCALE SIZE; RECONSTRUCTION METHOD; THREE-DIMENSIONAL IMAGE RECONSTRUCTION; THREE-DIMENSIONAL RECONSTRUCTION; THREE-DIMENSIONAL STRUCTURE; VIRAL NANOPARTICLES;

AMINO ACIDS; BACTERIOPHAGES; ELECTRON MICROSCOPES; IMAGE RECONSTRUCTION; NANOTECHNOLOGY; NANOTUBES; OLIGOMERS; THREE DIMENSIONAL;

PROTEINS;

BACTERIAL PROTEIN; COAT PROTEIN; DECORATION PROTEIN; GOLD DERIVATIVE; NANOGOLD; NANOTUBE; OLIGOMER; POLYHISTIDINE TAG; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; BACTERIOPHAGE P22; BETA SHEET; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONJUGATION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; NANOANALYSIS; NANOTECHNOLOGY; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE;

BACTERIOPHAGE P22; MATERIALS TESTING; NANOCAPSULES; NANOTUBES; PEPTIDE LIBRARY; PHARMACEUTICAL VEHICLES; VIRAL PROTEINS;

MIRIDAE;

EID: 84861225952     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2012.04.026     Document Type: Article

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