title: Analysis of protein folding and function using backbone modified proteins.
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.
authors.affiliation: Department of Chemistry, Duke University, Durham, NC 27708, USA.
authors.forename: Xiaoye
authors.initials: X
authors.lastname: Yang
authors.forename: Min
authors.initials: M
authors.lastname: Wang
authors.forename: Michael C
authors.initials: MC
authors.lastname: Fitzgerald
mesh_terms: D004952:Esters / Q000737:chemistry*; D006860:Hydrogen Bonding; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D004952:Esters; D011506:Proteins