Bis-ANS fluorescence of SpTrx WT and F26 mutants.

• 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.g005

Temperature-induced unfolding of SpTrx WT and F26 mutants were measured using bis-ANS fluorescence after incubating the proteins (10 μM) at various temperatures (4–90°C) for 2 h (excitation at 385 nm). The data presented are the means of three experiments.