50th Anniversary of the Molten Globule Prediction: The Impact on the Protein Folding Problem

Dear Colleagues,

Understanding of functionality of globular proteins is linked to the well-known structure-function paradigm. Unique protein structure defines specific function. Since a protein, and specifically water-soluble globular protein can spontaneously fold from the structure-less state (of a not yet completely synthesised chain at the ribosome, or unfolded, either in vivo or in vitro state), the information about its unique 3D structure (and, therefore, function) is encoded in its amino acid sequence. Not surprisingly, protein unfolding-refolding studies contributed significantly to our current understanding of the protein structure-based functionality. Early studies on protein unfolding and refolding were mostly based on the idea (supported by some experiments) that the process, at least for small proteins and protein domains, represents a two-state transition between folded and unfolded state, whereas accumulation of intermediates during protein unfolding was regarded as an exception to the rule. The existence of the partially folded intermediates that represents crucial steps in the protein folding process was foreseen in 1973 by Oleg B. Ptitsyn (1929-1999) based on the theoretical considerations of the potential mechanisms by which hierarchical structure of a native globular protein can be rapidly formed despite the astronomically large number of possibilities by which a polypeptide chain can be packed in a compact globule. Thereby, the existence of a crucial folding intermediate, which is expected to be formed during the protein folding, is characterized by high compactness, high content of usually native-like secondary structure and absence of unique tertiary structure was predicted. Later, it became famous under the name “molten globule”. Subsequent studies provided strong support to this Ptitsyn’s hypothesis, and the molten globule state was experimentally found and structurally characterized for many globular proteins. As a result, it became clear that the molten globule is crucial for protein folding.

This Special Issue is dedicated to the 50^th anniversary of the prediction of the existence of partially folded intermediates (including molten globule) that are formed during the protein folding. We are welcoming contributions from the researchers working on different aspects of partially folded proteins.

Prof. Dr. Vladimir N. Uversky
Prof. Dr. Alexei V. Finkelstein
Guest Editors

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