Premium
A PEG‐Based Oligomer as a Backbone Replacement for Surface‐Exposed Loops in a Protein Tertiary Structure
Author(s) -
Reinert Zachary E.,
Musselman Eli D.,
Elcock Adrian H.,
Horne W. Seth
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200200
Subject(s) - protein tertiary structure , peg ratio , oligomer , ethylene glycol , molecular dynamics , chemistry , residue (chemistry) , biophysics , biocompatible material , polymer chemistry , biochemistry , organic chemistry , computational chemistry , biology , medicine , finance , biomedical engineering , economics
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.