title: The internal structure of helical pores self-assembled from dendritic dipeptides is stereochemically programmed and allosterically regulated.
authors.affiliation: Roy and Diana Vagelos Laboratories, Department of Chemistry, Laboratory for Research on the Structure of Matter, University of Pennsylvania, Philadelphia, PA 19104-6323, USA. percec@sas.upenn.edu
authors.forename: Virgil
authors.initials: V
authors.lastname: Percec
authors.forename: Andrés E
authors.initials: AE
authors.lastname: Dulcey
authors.forename: Mihai
authors.initials: M
authors.lastname: Peterca
authors.forename: Monica
authors.initials: M
authors.lastname: Ilies
authors.forename: Janine
authors.initials: J
authors.lastname: Ladislaw
authors.forename: Brad M
authors.initials: BM
authors.lastname: Rosen
authors.forename: Ulrica
authors.initials: U
authors.lastname: Edlund
authors.forename: Paul A
authors.initials: PA
authors.lastname: Heiney
mesh_terms: D000494:Allosteric Regulation; D002942:Circular Dichroism; D050091:Dendrimers / Q000737:chemistry*; D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D050866:Liquid Crystals / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D016062:Porosity; D013237:Stereoisomerism; D014961:X-Ray Diffraction
chemical_list: D050091:Dendrimers; D004151:Dipeptides