Special Issue "Protein Folding 2013"

Guest Editor
Prof. Dr. Salvador Ventura
Protein Folding and Conformational Diseases Lab (PFCD), Dept. of Biochemistry and Molecular Biology, Institute of Biotechnology and Biomedicine, Parc de Recerca UAB, Mòdul B, Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), Spain
Website: http://ibb.uab.cat/ibb/index.php?option=com_wrapper&Itemid=143&CodiGrup=36
E-Mail: salvador.ventura@uab.es
Interests: protein folding; protein misfolding and aggregation; protein-protein interactions

Dear Colleagues,

Protein folding is among the most complex and challenging processes in Biochemistry. It is accepted that, after the synthesis at the ribosome, most polypeptides must fold into their specific three-dimensional structures before they can exert any biological function. Only properly folded conformers can interact specifically with their molecular targets. Therefore, protein folding is central to many biological processes. It has long been known that the functional structure of a protein is coded by its primary one-dimensional amino acid sequence. Despite the molecular mechanisms behind the folding code are still not completely understood, it is also true that in recent years we have witnessed significant advances towards this goal, resulting from the development of new experimental approaches and sophisticated prediction methods, but specially arising from new ways of thinking about protein folding and dynamics. Folding within biomembranes, multi-domain protein folding, folding in the cell, molecular chaperone-assisted holding and the dynamics of intrinsically disordered proteins are among the newest and more active areas of research. Although protein folding and dynamics are behind virtually all cell reactions, ranging from transcription to motion, it is the link to human disease that has put this subject in the public eye, because protein misfolding and subsequent aggregation have been shown to be the cause underlying dozens of human disorders. It turns out that understanding and predicting protein folding would allow elucidating how misfolded proteins cause aggregation and cytotoxicity. Thus, in a scientific environment that promotes technology transfer and tends to leave basic since aside, it is encouraging to learn that first principles hold the clue for therapeutic intervention in devastating disorders such us Parkinson’s and Alzheimer’s diseases. 
The aim of this special issue is to illustrate, through selected works, frontier research in protein folding.

Prof. Dr. Salvador Ventura
Guest Editor

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• amyloid
• calorimetry
• chaperones
• crowding and folding
• downhill folding
• energy lanscape
• folding in biomembranes
• folding in the cell
• folding intermediates
• folding kinetics
• intrinsically disordered proteins
• molecular dynamics simulation of folding
• oxidative folding
• protein aggregation
• protein folding and design
• protein folding and docking
• protein folding and evolution
• protein misfolding
• single molecule folding
• transition state analysis