Urea-induced unfolding curves 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.g004

Fluorescence spectra were measured after incubating the proteins with different concentrations of urea (0–10 M) at 25°C for 30 min (excitation at 280 nm). Data presented are means ± S.D. of three experiments.