Optimizing the fold stability of the circularly permuted Trp-cage motif.
Biopolymers
; 110(12): e23327, 2019 Dec.
Article
em En
| MEDLINE
| ID: mdl-31479150
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Modelos Moleculares
/
Dobramento de Proteína
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article