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

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (15 September 2023) | Viewed by 155

Special Issue Editors

Department of Molecular Medicine, USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd, MDC07, Tampa, FL 33612, USA
Interests: intrinsically disordered proteins; protein folding; protein misfolding; partially folded proteins; protein aggregation; protein structure; protein function; protein stability; protein biophysics; protein bioinformatics; conformational diseases; protein–ligand interactions; protein–protein interactions; liquid-liquid phase transitions
Special Issues, Collections and Topics in MDPI journals
Laboratory of Protein Physics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Interests: protein physics; protein structure; protein folding; protein folding intermediates; protein design; phase transitions; phase transition kinetics; transition states; antifreeze proteins; amyloids; protein bioinformatics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

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 50th 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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • protein folding
  • cotranslational folding
  • chaperone-assisted folding
  • protein denaturation
  • protein unfolding
  • protein refolding
  • partially folded protein
  • folding intermediate
  • molten globule
  • protein misfolding
  • protein aggregation
  • conformational disease

Published Papers

There is no accepted submissions to this special issue at this moment.
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