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Correction

Correction: Ca2+ Binding Enhanced Mechanical Stability of an Archaeal Crystallin

  • The PLOS ONE Staff
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Figure 1 is incorrectly printed in black and white. Please see the correct Figure 1 here.

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Figure 1. Structure and 2D topology diagram of two β-sandwich proteins with Greek key motifs used in this study.

The pulling direction used in the single-molecule force spectroscopy (SMFS) experiments is shown by arrows. (A) NMR structure of I27 (PDB ID: 1TIT). Terminal β-strands A′ and G are directly connected by H-bonding, shearing this “mechanical-clamp” results in the mechanical unfolding of the protein. The rupture of H-bonds between A and B strands constitutes the less stable mechanical intermediate. (B) 2D topology diagram of I27. The five-stranded (BCDEF) ‘double’ Greek key (3,2)3 formed by overlapping (3,1)N and (2,2)C Greek keys (as defined by Hutchinson and Thornton [53]). (C) NMR structure of M-crystallin (PDB ID: 2K1W) bound to two Ca2+ ions (shown as black spheres). The terminal β-strands A and H are not directly bonded and they need to be “peeled” away from each other to unfold the protein. (D) 2D topology diagram of M-crystallin showing the two (3,1)C Greek keys formed by ABCD and EFGH. In both cases, the backbone H-bonding around the terminal strands is shown.

https://doi.org/10.1371/journal.pone.0094513.g001

Reference

  1. 1. Ramanujam V, Kotamarthi HC, Ainavarapu SRK (2014) Ca2+ Binding Enhanced Mechanical Stability of an Archaeal Crystallin. PLoS ONE 9(4): e94513

Citation: The PLOS ONE Staff (2014) Correction: Ca2+ Binding Enhanced Mechanical Stability of an Archaeal Crystallin. PLoS ONE 9(7): e102924. https://doi.org/10.1371/journal.pone.0102924

Published: July 11, 2014

Copyright: © 2014 The PLOS ONE Staff. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.