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

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 l...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2012-05, Vol.13 (8), p.1107-1111
Main Authors: Reinert, Zachary E., Musselman, Eli D., Elcock, Adrian H., Horne, W. Seth
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Biomimetic Materials - chemistry
Circular Dichroism
Crystallization
Models, Molecular
Molecular Sequence Data
peptide mimics
poly(ethylene glycol)
Polyethylene Glycols - chemistry
polymers
protein backbone
Protein Structure, Tertiary
proteins
Proteins - chemistry
Thermodynamics
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Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201200200