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Analysis of protein folding and function using backbone modified proteins.

Publication ,  Journal Article
Yang, X; Wang, M; Fitzgerald, MC
Published in: Bioorganic chemistry
October 2004

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.

Duke Scholars

Published In

Bioorganic chemistry

DOI

EISSN

1090-2120

ISSN

0045-2068

Publication Date

October 2004

Volume

32

Issue

5

Start / End Page

438 / 449

Related Subject Headings

  • Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Organic Chemistry
  • Mutation
  • Hydrogen Bonding
  • Esters
  • 3405 Organic chemistry
  • 3404 Medicinal and biomolecular chemistry
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Yang, X., Wang, M., & Fitzgerald, M. C. (2004). Analysis of protein folding and function using backbone modified proteins. Bioorganic Chemistry, 32(5), 438–449. https://doi.org/10.1016/j.bioorg.2004.06.011
Yang, Xiaoye, Min Wang, and Michael C. Fitzgerald. “Analysis of protein folding and function using backbone modified proteins.Bioorganic Chemistry 32, no. 5 (October 2004): 438–49. https://doi.org/10.1016/j.bioorg.2004.06.011.
Yang X, Wang M, Fitzgerald MC. Analysis of protein folding and function using backbone modified proteins. Bioorganic chemistry. 2004 Oct;32(5):438–49.
Yang, Xiaoye, et al. “Analysis of protein folding and function using backbone modified proteins.Bioorganic Chemistry, vol. 32, no. 5, Oct. 2004, pp. 438–49. Epmc, doi:10.1016/j.bioorg.2004.06.011.
Yang X, Wang M, Fitzgerald MC. Analysis of protein folding and function using backbone modified proteins. Bioorganic chemistry. 2004 Oct;32(5):438–449.
Journal cover image

Published In

Bioorganic chemistry

DOI

EISSN

1090-2120

ISSN

0045-2068

Publication Date

October 2004

Volume

32

Issue

5

Start / End Page

438 / 449

Related Subject Headings

  • Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Organic Chemistry
  • Mutation
  • Hydrogen Bonding
  • Esters
  • 3405 Organic chemistry
  • 3404 Medicinal and biomolecular chemistry