Literature DB >> 15355097

Backbone thioester exchange: a new approach to evaluating higher order structural stability in polypeptides.

Matthew G Woll1, Samuel H Gellman.   

Abstract

An amide bond has been replaced by a thioester in bovine pancreatic polypeptide (bPP) to allow rapid and reversible (dynamic) exchange of the alpha-helical segment with other thiols in solution. We have begun to study the higher order structural stability of bPP by measuring the equilibrium constant of the "backbone thioester exchange" (BTE) reaction. The extent to which the equilibrium (KBTE) favors one set of peptides over the other, which can be easily measured, can be directly correlated to the energy gained from favorable noncovalent interactions that occur between peptide segments on either side of the thioester bond (Kfold).

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Year:  2004        PMID： 15355097     DOI： 10.1021/ja046891i

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


  13 in total

1.  Preferred side-chain constellations at antiparallel coiled-coil interfaces.

Authors:  Erik B Hadley; Oliver D Testa; Derek N Woolfson; Samuel H Gellman
Journal:  Proc Natl Acad Sci U S A       Date:  2008-01-09       Impact factor: 11.205

2.  The relative rates of thiol-thioester exchange and hydrolysis for alkyl and aryl thioalkanoates in water.

Authors:  Paul J Bracher; Phillip W Snyder; Brooks R Bohall; George M Whitesides
Journal:  Orig Life Evol Biosph       Date:  2011-07-05       Impact factor: 1.950

3.  Strong contributions from vertical triads to helix-partner preferences in parallel coiled coils.

Authors:  Jay D Steinkruger; Gail J Bartlett; Derek N Woolfson; Samuel H Gellman
Journal:  J Am Chem Soc       Date:  2012-09-13       Impact factor: 15.419

4.  The d'--d--d' vertical triad is less discriminating than the a'--a--a' vertical triad in the antiparallel coiled-coil dimer motif.

Authors:  Jay D Steinkruger; Gail J Bartlett; Erik B Hadley; Lindsay Fay; Derek N Woolfson; Samuel H Gellman
Journal:  J Am Chem Soc       Date:  2012-01-31       Impact factor: 15.419

5.  Native chemical ligation of thioamide-containing peptides: development and application to the synthesis of labeled α-synuclein for misfolding studies.

Authors:  Solongo Batjargal; Yanxin J Wang; Jacob M Goldberg; Rebecca F Wissner; E James Petersson
Journal:  J Am Chem Soc       Date:  2012-04-02       Impact factor: 15.419

6.  Side-chain pairing preferences in the parallel coiled-coil dimer motif: insight on ion pairing between core and flanking sites.

Authors:  Jay D Steinkruger; Derek N Woolfson; Samuel H Gellman
Journal:  J Am Chem Soc       Date:  2010-06-09       Impact factor: 15.419

7.  Infrared study of the folding mechanism of a helical hairpin: porcine PYY.

Authors:  Matthias M Waegele; Feng Gai
Journal:  Biochemistry       Date:  2010-09-07       Impact factor: 3.162

8.  Detection and analysis of chimeric tertiary structures by backbone thioester exchange: packing of an alpha helix against an alpha/beta-peptide helix.

Authors:  Joshua L Price; Erik B Hadley; Jay D Steinkruger; Samuel H Gellman
Journal:  Angew Chem Int Ed Engl       Date:  2010       Impact factor: 15.336

9.  In situ monitoring of backbone thioester exchange by 19F NMR.

Authors:  William C Pomerantz; Erik B Hadley; Charles G Fry; Samuel H Gellman
Journal:  Chembiochem       Date:  2009-09-04       Impact factor: 3.164

10.  Helix Propensities of Amino Acid Residues via Thioester Exchange.

Authors:  Brian F Fisher; Seong Ho Hong; Samuel H Gellman
Journal:  J Am Chem Soc       Date:  2017-09-12       Impact factor: 15.419
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