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. Author manuscript; available in PMC: 2013 Jun 26.
Published in final edited form as: Biochemistry. 2012 Jun 15;51(25):5105–5112. doi: 10.1021/bi300525x

Figure 2.

Figure 2

A) Superposition of subunits from Hsp16.5-P1 (red and blue) and Hsp16.5-WT (gray) demonstrates that the α-crystallin domain fold is conserved and highlights the change in orientation of the C-terminal tail in one of the Hsp16.5-P1 subunits. B) Ribbon diagram of the dimer from Hsp16.5-P1 (red and blue) superimposed on the dimer from Hsp16.5-WT (gray) shows that that oligomer expansion does not perturb the interface of the dimer involving stand swapping (strand 6) and extensive networks of contacts between loops.