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Ajitha S. Cristie-David
Researcher at University of Michigan
Publications - 9
Citations - 150
Ajitha S. Cristie-David is an academic researcher from University of Michigan. The author has contributed to research in topics: Coiled coil & Protein design. The author has an hindex of 5, co-authored 9 publications receiving 104 citations.
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Journal ArticleDOI
Coiled-Coil-Mediated Assembly of an Icosahedral Protein Cage with Extremely High Thermal and Chemical Stability.
Ajitha S. Cristie-David,Junjie Chen,Derek Nowak,Amy L. Bondy,Kai Sun,Sung Park,Mark M. Banaszak Holl,Min Su,E. Neil G. Marsh +8 more
TL;DR: The cage was constructed based on icosahedral symmetry by genetically fusing a trimeric protein to a small pentameric de novo-designed coiled coil domain, separated by a flexible oligo-glycine linker sequence and proved to be extremely stable toward thermal and chemical denaturation.
Journal ArticleDOI
Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils
Somayesadat Badieyan,Aaron Sciore,Joseph D. Eschweiler,Philipp Koldewey,Ajitha S. Cristie-David,Brandon T. Ruotolo,James C.A. Bardwell,Min Su,E. Neil G. Marsh +8 more
TL;DR: This work demonstrates the assembly of a trimeric enzyme into a well‐defined tetrahedral cage by genetically fusing a trimmederic coiled‐coil domain to its C terminus through a flexible polyglycine linker sequence.
Journal ArticleDOI
Evaluation of de novo-designed coiled coils as off-the-shelf components for protein assembly
Ajitha S. Cristie-David,Aaron Sciore,Somayesadat Badieyan,Joseph D. Escheweiler,Philipp Koldewey,James C.A. Bardwell,James C.A. Bardwell,Brandon T. Ruotolo,E. Neil G. Marsh +8 more
TL;DR: This work investigates the ability of a series of well-characterized de novo-designed parallel coiled coils, with oligomerization states ranging from dimer to pentamer, to mediate the oligomersization of a model monomeric protein, green fluorescent protein (GFP).
Journal ArticleDOI
Metal-dependent assembly of a protein nano-cage
TL;DR: Characterization of the assembled protein indicated that the metal ion–protein complex formed discrete globular structures of the diameter expected for a complex containing 12 copies of the protein monomer.
Journal ArticleDOI
Elaborating a coiled-coil-assembled octahedral protein cage with additional protein domains.
Ajitha S. Cristie-David,Philipp Koldewey,Ben A. Meinen,James C.A. Bardwell,James C.A. Bardwell,E. Neil G. Marsh +5 more
TL;DR: This study shows the potential of using small, coiled‐coil motifs as off‐the‐shelf components to design MDa‐sized protein cages to which additional structural or functional elements can be added in a modular manner.