Analysis of protein folding and function using backbone modified proteins.

Journal Article (Review;Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Yang, X; Wang, M; Fitzgerald, MC

Published Date

  • October 2004

Published In

Volume / Issue

  • 32 / 5

Start / End Page

  • 438 - 449

PubMed ID

  • 15381405

Electronic International Standard Serial Number (EISSN)

  • 1090-2120

International Standard Serial Number (ISSN)

  • 0045-2068

Digital Object Identifier (DOI)

  • 10.1016/j.bioorg.2004.06.011


  • eng