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.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Biomimetic Materials / chemistry*
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Circular Dichroism
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Crystallization
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Models, Molecular
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Molecular Sequence Data
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Polyethylene Glycols / chemistry*
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Protein Structure, Tertiary
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Proteins / chemistry*
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Thermodynamics
Substances
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Bacterial Proteins
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IgG Fc-binding protein, Streptococcus
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Proteins
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Polyethylene Glycols