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- Subunit Conformations and Assembly States of a DNA-translocating Motor: The Terminase of
- seawater (Fig. 2), according to the following relationship.
- The P22 Tail Machine at Subnanometer Resolution Reveals the Architecture of an Infection Conduit
- Structural Transformations Accompanying the Assembly of Bacteriophage P22 Portal Protein Rings in Vitro*
- Cavity Defects in the Procapsid of Bacteriophage P22 and the Mechanism of Capsid Maturation
- An Aggregation-Prone Intermediate Species Is Present in the Unfolding Pathway of the Monomeric Portal Protein of Bacteriophage P22: Implications for Portal
- Identification of Novel Interactions in HIV-1 Capsid Protein Assembly by High-resolution
- Three-dimensional structure of the bacteriophage P22 tail machine
- Probing Conserved Helical Modules of Portal Complexes by Mass Spectrometry-based
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- Domain Study of Bacteriophage P22 Coat Protein and Characterization of the Capsid Lattice Transformation
- Solution X-Ray Scattering-Based Estimation of Electron Cryomicroscopy Imaging Parameters for Reconstruction of Virus Particles
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- Identification of Subunit-Subunit Interactions in Bacteriophage P22 Procapsids by Chemical Cross-linking and Mass Spectrometry
- Controlled Assembly of Bifunctional Chimeric Protein Cages and Composition Analysis Using Noncovalent Mass Spectrometry
- Macromolecular mass spectrometry and electron microscopy as complementary tools for investigation of the heterogeneity
- Molecular Dissection of 29 Scaffolding Protein Function in an in Vitro Assembly System
- In vitro incorporation of the phage Phi29 connector complex Chi-yu Fu, Peter E. Prevelige Jr.
- Synthesis of biotin-tagged chemical cross-linkers and their applications for mass spectrometry
- DOI: 10.1002/cbic.200700555 Development of Bacteriophage P22 as a Platform for Molecular Display
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- Incorporation of scaffolding protein gpO in bacteriophages P2 and P4 Jenny R. Chang a,b
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- Structure of Bacteriophage P22 Portal Protein in Relation to Assembly: Investigation by Raman Spectroscopy
- Kinetic and Calorimetric Evidence for Two Distinct Scaffolding Protein Binding Populations within the Bacteriophage P22 Procapsid
- COMMUNICATION Hydrogen-deuterium Exchange as a Probe of Folding
- Characterization of Subunit Structural Changes Accompanying Assembly of the Bacteriophage P22 Procapsid
- Structure of the Coat Protein-binding Domain of the Scaffolding Protein from a Double-stranded DNA Virus
- Visualization of the Maturation Transition in Bacteriophage P22 by Electron Cryomicroscopy
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- Identification and Characterization of the Domain Structure of Bacteriophage P22 Coat Protein
- Mechanism of Scaffolding-Directed Virus Assembly Suggested by Comparison of Scaffolding-Containing and Scaffolding-Lacking
- Viral disease continues to cause significant human suf-fering and economic loss. Vaccination is an extremely
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- Preliminary crystallographic analysis of the bacteriophage P22 portal protein
- Detection of Intermediates and Kinetic Control during Assembly of Bacteriophage P22 Procapsid
- Bacteriophage P22 Portal Vertex Formation in Vivo Sean D. Moore and Peter E. Prevelige Jr*
