Implication of Molten Globule on the Function and Toxicity of a Protein

Abstract

Molten globule (MG) are the compact globules with significant amount of native secondary structure and a relatively higher side chain mobility compared to native form, stabilized by non-specific hydrophobic interactions. MG states are better understood in the context of the protein folding process existing as the intermediate states. The MG state was long believed to be a non-active state of protein owing to the loss of tertiary structure and different folding than the native state. A better understanding of MG structures in the recent years have however revealed the functional roles of MG states. The MG states are majorly involved in the functioning of biological processes by existing at various intermediate levels during the protein folding or unfolding processes. Majorly, MG functional roles are involved in cellular processes, protein–ligand interaction, enzymatic activity, assisting chaperones, membrane penetration of proteins, translocation of toxins and genetic diseases involving misfolded proteins. The unraveling of the roles of the MG state in the cellular processes will prove to be effective in the design of antidotes as well as diagnostics to counteract effects of various toxins. The understanding of the functional roles of the MG is also vital for the basic understanding of folding pathways and enzymatic activities of the proteins involved.