title: A PEG-based oligomer as a backbone replacement for surface-exposed loops in a protein tertiary structure.
abstract: PEGged out: Poly(ethylene glycol), a simple biocompatible polymer, can replace natural loop segments in a 56-residue protein domain with a well-defined tertiary structure. Biophysical characterization of chimeras of the protein GB1 coupled with molecular dynamics simulations show that PEG enhances local backbone torsional freedom without compromising the overall protein fold or function.
authors.affiliation: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
authors.forename: Zachary E
authors.initials: ZE
authors.lastname: Reinert
authors.forename: Eli D
authors.initials: ED
authors.lastname: Musselman
authors.forename: Adrian H
authors.initials: AH
authors.lastname: Elcock
authors.forename: W Seth
authors.initials: WS
authors.lastname: Horne
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D040761:Biomimetic Materials / Q000737:chemistry*; D002942:Circular Dichroism; D003460:Crystallization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011092:Polyethylene Glycols / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D011506:Proteins; D011092:Polyethylene Glycols