Skip to main content
. Author manuscript; available in PMC: 2019 Oct 1.
Published in final edited form as: Biochim Biophys Acta. 2015 Sep 2;1860(1 Pt B):240–245. doi: 10.1016/j.bbagen.2015.08.014

FIGURE 5: Model for the interactive sequences in a ribbon model of the small heat shock protein, human alphaB crystallin.

FIGURE 5:

Possibly the most surprising result of the study of the interactive sequences in human alphaB crystallin was the identification of multiple interactive sequences. The sequences form a diverse network of potential protective sites for selective interaction with several categories of target proteins. The biological, biophysical and pharmacological advantages of combining a number of multifunctional interactive sites on a single intracellular protective molecule, instead of numerous soluble cytoplasmic peptides, as small as four amino acids, each with protective activity remains to be determined.