ISSN 0006-2979, Biochemistry (Moscow), 2025, Vol. 90, No. 2, p. 300-301 © Pleiades Publishing, Ltd., 2025.
300
ERRATUM
Erratum to: Denaturation Properties and Folding
Transition States of Leghemoglobin
and Other Heme Proteins
Pijush Basak
1
, Niloy Kundu
2
, Rudradip Pattanayak
1
,
and Maitree Bhattacharyya
1
*
1
Department of Biochemistry, University of Calcutta,
35 Ballygunge Circular Road, Kolkata-700019, India; fax: +91 (33) 2461-4849
2
Department of Chemistry, Indian Institute of Technology,
Kharagpur-721302, India; fax: +91 (32) 2228_2252
a
e-mail: bmaitree@gmail.com
Received September 25, 2014
Revised November 20, 2014
Accepted November 20, 2014
DOI: 10.1134/S0006297925020026
The original article can be found online at https://doi.org/10.1134/S0006297915040100
In the published article by Basak et al. Figures 4 and 5 were given incorrectly. The Editorial Office would like
to correct the figures with legends and apologizes for any inconvenience that it may have caused.
Figure 4 should be corrected as follows:
Fig. 4. Change in free energy for Leghemoglobin unfolding as a function of Urea(a) and guanidine hydrochloride(b) concen-
tration. The experimental values of ∆G
D
was derived from Equations (1) and (2) during unfolding transition measurement.
Theextrapolation of the line represents ∆G
D,H20
for Urea=0.56 Kcal·mol
−1
and ∆G
D,H20
for GdnHCl=1.70Kcal·mol
−1
.
ERRATUM 301
BIOCHEMISTRY (Moscow) Vol. 90 No. 2 2025
Figure 5 should be corrected as follows:
Fig. 5. Change in free energy for Myoglobin unfolding as a function of Urea(a) and guanidine hydrochloride(b) concentration.
The experimental values of ∆G
D
was derived from Equation(1) and(2) during unfolding transition measurement. The extrapola-
tion of the line represents ∆G
D,H20
for Urea=3.00Kcal·mol
−1
and ∆G
D,H20
for GdnHCl=2.268Kcal·mol
−1
.
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