A PEG-based oligomer as a backbone replacement for surface-exposed loops in a protein tertiary structure

Chembiochem. 2012 May 29;13(8):1107-11. doi: 10.1002/cbic.201200200. Epub 2012 Apr 26.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Biomimetic Materials / chemistry*
  • Circular Dichroism
  • Crystallization
  • Models, Molecular
  • Molecular Sequence Data
  • Polyethylene Glycols / chemistry*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Thermodynamics

Substances

  • Bacterial Proteins
  • IgG Fc-binding protein, Streptococcus
  • Proteins
  • Polyethylene Glycols