Special Issue "Protein Folding"

Guest Editor
Dr. Andrei Alexandrescu
Molecular & Cell Biology, University of Connecticut, BSP 209, 91 North Eagleville Road, Unit 3125, Storrs, CT 06269-3125, USA
Website: http://mcb.uconn.edu/fac.php?name=alexandrescuat
E-Mail:
Interests: protein folding; amyloids; alzheimer's disease; parkinson's disease; type II diabetes; structural biology; nuclear magnetic resonance spectroscopy; structural bioinformatics; protein misfolding; neuromuscular junction proteins; OB-fold proteins; protein dynamics; biophysics

Editorial Advisor
Prof. Dr. Martin Gruebele
Department of Chemistry, University of Illinois, A220 Chemical & Life Sciences Lab, 600 South Mathews Avenue, Urbana, IL 61801, USA
Website: http://www.scs.uiuc.edu/chem/faculty/Martin_Gruebele.html
E-Mail:
Interests: protein folding; RNA folding; downhill folding; protein-protein interactions; biomolecular simulation; temperature jump; small angle X-ray scattering

Dear Colleagues,

In recent years protein folding often seems to have become synonymous with protein structure prediction. The field of protein folding is in fact considerably more encompassing than the ability to stitch together recurrent structural motifs into models that come closer to a target than those of competitors. The targets are moving, and as predictions become more sophisticated with each passing tournament, so does our appreciation of the intricacies of protein structure, function, and dynamics.

The papers in this issue highlight work at the frontiers of protein folding research. Topics include the behaviors of proteins under extreme or non-physiological environments such as the interactions of proteins with surfaces, synthetic matrices, chaotropes and kosmotropes, and the sheltering environment of chaperones. The mechanisms by which protein misfolding leads to disease remains a challenging and medically important problem. New experimental approaches and new ways of thinking about protein folding are described. And finally, there are papers that continue to address the fundamental unresolved problem of how protein sequences encode for the three-dimensional structures of proteins.

In a climate that often emphasizes the "biology" bottom line, it is refreshing to see basic science flourishing and needed as much as ever in research that may not translate to a pharmaceutical pill but that has and will continue to reveal fundamental insights into the roles of molecular structures in health and disease. Yes, protein folding has been "solved" many times over but it keeps presenting interesting problems and opportunities that should continue to challenge the most ambitious investigators for years to come.

Andrei Alexandrescu
Guest Editor

Submission

All papers should be submitted to ijms@mdpi.org. To be published continuously until the deadline and papers will be listed together at the special issue website.

Submitted papers should not have been published previously, nor be under consideration for publication elsewhere. All papers are refereed through a peer-review process. A guide for authors is available on the Instructions for Authors page. The International Journal of Molecular Sciences is an international peer-reviewed monthly journal published by Molecular Diversity Preservation International.

Open Access publication fees are 800 CHF per paper. English correction fees and/or formatting fees (250 CHF) will be added in certain cases (1050 CHF per paper for those papers that require extensive additional formatting and/or English corrections).

• Folding and docking/binding
• Protein misfolding
• Protein folding and transient aggregation
• MD simulation of folding
• Folding heterogeneity and intermediates
• Energy landscapes, analysis
• Energy landscapes, computation
• Dynamics and kinetics, experiments
• Single molecule folding, spectroscopy
• Single molecule folding, force
• Elementary reactions, secondary structure
• Downhill folding
• Calorimetric folding/unfolding
• Protein folding and design
• Protein folding and evolution
• Protein dynamics computation, vibrational dynamics
• Chaperoning and in vivo folding
• Transition state analysis
• Crowding and folding