Abstract:
: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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Graham KA,Byrne A,Mason M,Andersen NHdoi
10.1002/bip.23327subject
Has Abstractpub_date
2019-12-01 00:00:00pages
e23327issue
12eissn
0006-3525issn
1097-0282journal_volume
110pub_type
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