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A PEG‐Based Oligomer as a Backbone Replacement for Surface‐Exposed Loops in a Protein Tertiary Structure
Journal article   Peer reviewed

A PEG‐Based Oligomer as a Backbone Replacement for Surface‐Exposed Loops in a Protein Tertiary Structure

Zachary E Reinert, Eli D Musselman, Adrian H Elcock and W. Seth Horne
Chembiochem : a European journal of chemical biology, Vol.13(8), pp.1107-1111
05/29/2012
DOI: 10.1002/cbic.201200200
PMID: 22539233

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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.
peptide mimics protein backbone polymers poly(ethylene glycol) proteins

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