Bis-ANS fluorescence of SpTrx WT and F26 mutants.

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.

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.g005
Description
Summary: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.

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