Urea-induced unfolding curves of SpTrx WT and F26 mutants.

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.

Bibliographic Details
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

Description
Summary:	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.