Analysis of protein folding and function using backbone modified proteins |
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Authors: | Yang Xiaoye Wang Min Fitzgerald Michael C |
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Affiliation: | Department of Chemistry, Duke University, Durham, NC 27708, USA. |
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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. |
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Keywords: | Analogues Protein systems |
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