Sergio
Romero-Romero
a,
Miguel
Costas
b,
Adela
Rodríguez-Romero
c and
D. Alejandro
Fernández-Velasco
*a
aLaboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, 04510 Ciudad de México, Distrito Federal, Mexico. E-mail: fdaniel@unam.mx
bLaboratorio de Biofisicoquímica, Departamento de Fisicoquímica, Facultad de Química, Universidad Nacional Autónoma de México, 04510 Ciudad de México, Distrito Federal, Mexico
cLaboratorio de Química de Biomacromoléculas 3, Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, 04510 Ciudad de México, Distrito Federal, Mexico
First published on 24th March 2016
Correction for ‘Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins’ by Sergio Romero-Romero et al., Phys. Chem. Chem. Phys., 2015, 17, 20699–20714.
The size of the biggest cavity, located at the interface between β-strands 4–6 and α-helices 4–6 (comprising residues 90–120, 145–160 and 195–200; Fig. S6, ESI‡), is the main responsible of the cavity volume difference between RevTIMs and IrrevTIMs (Table 4 and Fig. 7).
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
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