Abstract:
:Protein engineers traditionally rely on amino acid substitutions to alter the functional properties of biomacromolecules, yet have largely overlooked the potential benefits of reorganizing the polypeptide chain of a protein by circular permutation (CP). By connecting the native protein termini via a covalent linker and introducing new ends through the cleavage of an existing peptide bond, CP can perturb local tertiary structure and protein dynamics, as well as introduce possible quaternary structure changes. In several recent studies, these effects have successfully been exploited to manipulate protein scaffolds, resulting in improved catalytic activity and altered substrate or ligand binding affinity, as well as enabling the design of novel biocatalysts and biosensors.
journal_name
Trends Biotechnoljournal_title
Trends in biotechnologyauthors
Yu Y,Lutz Sdoi
10.1016/j.tibtech.2010.10.004subject
Has Abstractpub_date
2011-01-01 00:00:00pages
18-25issue
1eissn
0167-7799issn
1879-3096pii
S0167-7799(10)00178-2journal_volume
29pub_type
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