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Optimizing the fold stability of the circularly permuted Trp-cage motif.

08:00 EDT 3rd September 2019 | BioPortfolio

Summary of "Optimizing the fold stability of the circularly permuted Trp-cage motif."

Through optimization of the linker region and key stabilizing mutations, it has been possible to improve the stability of the circularly permuted (cp) Trp-cage miniprotein. However, even the most stable Trp-cage circular permutants are still less stable than the analogous standard topology (std) Trp-cages. Extending mutational studies of Trp-cage fold stability to cp-species, including analogs lacking chain terminal charges, has uncovered and quantitated some additional stabilizing and destabilizing interactions. Upon protonation, the circular permutants are destabilized to a much greater extent than the standard topology series. End effects, particularly Coulombic interactions, appear to be more important for the cp-series while the Y10/P4 interaction in the cp-series is not as significant a stabilizing feature as the corresponding Y3/P19 in the standard topology series.

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This article was published in the following journal.

Name: Biopolymers
ISSN: 1097-0282
Pages: e23327

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Temperate bacteriophage of the genus INOVIRUS which infects enterobacteria, especially E. coli. It is a filamentous phage consisting of single-stranded DNA and is circularly permuted.

A species of temperate bacteriophage in the genus P1-like viruses, family MYOVIRIDAE, which infects E. coli. It is the largest of the COLIPHAGES and consists of double-stranded DNA, terminally redundant, and circularly permuted.

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An RNA-binding motif characterized by an alpha-beta-beta-beta-alpha fold that binds DOUBLE-STRANDED RNA. It occurs in many eukaryotic proteins as well as in bacterial and viral proteins.

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