Comparison of the thermal stability and conformational flexibility of two components of Trx system in Sphingomona s sp. PAMC 26621 and the fluorescence properties of phenylalanine mutants of SpTrx.

• Main Authors: Thu-Thuy Nguyen (9325402), Trang Hoang (676675), Kiet N. Tran (9099305), Hyeonji Kim (3839122), Sei-Heon Jang (2828522), ChangWoo Lee (2828525)
• Format: Still Image
• Language: unknown
• Published: 2021
• Subjects: Biophysics; Biochemistry; Molecular Biology; Biotechnology; Ecology; Environmental Sciences not elsewhere classified; Biological Sciences not elsewhere classified; Chemical Sciences not elsewhere classified; small redox protein; psychrophilic arctic bacterium; high temperatures regardless; f26a mutants resulted; div >< p; common structure consisting; aromatic amino acids; f26 mutants compared; exhibits thermal stability; aromatic residues; aromatic cluster; β2 terminus; study examined; studied extensively; structural stability; structural instability; sphingomonas </; spectroscopic investigations; site conformation; sheet flanked; results suggest; pamc 26621; induced unfolding; including psychrophiles; fully elucidated; f26 showed; f26 changed; central β; buried phenylalanine; buried inside; buried f26; aliphatic cluster; adapted organisms; Arctic
• Online Access: https://doi.org/10.1371/journal.pone.0261123.g003

(A) Fluorescence spectra of WT SpTrx and SpTR upon incubation of the proteins at various temperatures (4–70°C) for 2 h. (B) Acrylamide Stern-Volmer plot for WT SpTrx and SpTR. F 0 , the maximum fluorescence intensity without acrylamide; F, the maximum fluorescence intensity under increasing concentrations (0.1–0.5 M) of acrylamide. (C) Effect of tyrosine substitution in the aromatic cluster of SpTrx on protein fluorescence. The data are presented as the means of three experiments (A and C) or means ± S.D. of three experiments (B). Excitation at 280 nm.