Analysis of protein folding and function using backbone modified proteins

Bioorganic Chemistry
Xiaoye YangMichael C Fitzgerald

Abstract

With the recent development of chemical and biological methods to introduce backbone modifications into the polypeptide chains of proteins, there have been a growing number of site-directed mutagenesis experiments focused on understanding the role of the polypeptide backbone in protein folding and function. The substitution of a main chain amide bond with an ester bond is now a popular mutation to investigate the role of the polypeptide backbone in ligand, binding, enzyme catalysis, and protein folding. Here we review the results of studies on some 25 ester-bond containing analogues from nine different protein systems. The structural, thermodynamic, and functional consequences of introducing backbone amide- to ester-bond mutations into these protein systems are discussed.

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Citations

Mar 23, 2010·The Journal of Physical Chemistry. B·Takako Takeda, Dmitri K Klimov
Oct 17, 2013·Proceedings of the National Academy of Sciences of the United States of America·Kimberly MatulefFrancis I Valiyaveetil
Jun 25, 2010·Protein Engineering, Design & Selection : PEDS·Majid Masso, Iosif I Vaisman
Sep 12, 2006·Journal of Molecular Biology·Xiaoye YangMichael C Fitzgerald
May 13, 2006·Bioorganic Chemistry·Xiaoye Yang, Michael C Fitzgerald
Oct 9, 2007·Biopolymers·Jan SpenglerFernando Albericio
Dec 12, 2007·Angewandte Chemie·Jiantao GuoPeter G Schultz
Oct 30, 2013·Organic & Biomolecular Chemistry·Kuruppanthara N VijayadasGangadhar J Sanjayan
Mar 15, 2014·Chemical Society Reviews·Ilker AvanAlan R Katritzky
Jul 6, 2014·Beilstein Journal of Organic Chemistry·Angélica de Fátima S BarretoCarlos Kleber Z Andrade

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