Analysis of protein folding and function using backbone modified proteins.
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
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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
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Issue
Start / End Page
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