Literature DB >> 22539233

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

Zachary E Reinert1, Eli D Musselman, Adrian H Elcock, W Seth Horne.   

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.

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Year:  2012        PMID: 22539233     DOI: 10.1002/cbic.201200200

Source DB:  PubMed          Journal:  Chembiochem        ISSN: 1439-4227            Impact factor:   3.164


  10 in total

1.  The Surface of Protein λ6-85 Can Act as a Template for Recurring Poly(ethylene glycol) Structure.

Authors:  Shu-Han Chao; Jan Schäfer; Martin Gruebele
Journal:  Biochemistry       Date:  2017-10-06       Impact factor: 3.162

2.  Evidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domain.

Authors:  David E Mortenson; Dale F Kreitler; Hyun Gi Yun; Samuel H Gellman; Katrina T Forest
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2013-11-19

3.  Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.

Authors:  Kelly L George; W Seth Horne
Journal:  Acc Chem Res       Date:  2018-04-19       Impact factor: 22.384

4.  Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins.

Authors:  Yanxin J Wang; D Miklos Szantai-Kis; E James Petersson
Journal:  Org Biomol Chem       Date:  2016-06-06       Impact factor: 3.876

5.  Protein-like tertiary folding behavior from heterogeneous backbones.

Authors:  Zachary E Reinert; George A Lengyel; W Seth Horne
Journal:  J Am Chem Soc       Date:  2013-08-15       Impact factor: 15.419

Review 6.  Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure.

Authors:  Zachary E Reinert; W Seth Horne
Journal:  Org Biomol Chem       Date:  2014-11-28       Impact factor: 3.876

7.  Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.

Authors:  Zachary E Reinert; W Seth Horne
Journal:  Chem Sci       Date:  2014-08-01       Impact factor: 9.825

Review 8.  Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.

Authors:  Jacqueline R Santhouse; Shilpa R Rao; W Seth Horne
Journal:  Methods Enzymol       Date:  2021-05-03       Impact factor: 1.600

9.  The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts.

Authors:  Christopher R Walters; D Miklos Szantai-Kis; Yitao Zhang; Zachary E Reinert; W Seth Horne; David M Chenoweth; E James Petersson
Journal:  Chem Sci       Date:  2017-02-08       Impact factor: 9.825

10.  Towards "bionic" proteins: replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics.

Authors:  George M Burslem; Hannah F Kyle; Alexander L Breeze; Thomas A Edwards; Adam Nelson; Stuart L Warriner; Andrew J Wilson
Journal:  Chem Commun (Camb)       Date:  2016-04-07       Impact factor: 6.222

  10 in total

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