Analysis of protein folding and function using backbone modified proteins.

Journal Article (Review)

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

Pubmed Central 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