This month’s issue of Nature Structural & Molecular Biology offers a focus on protein folding with articles such as:

• Editorial: Folding to Function (pp573)
• Converging concepts of protein folding in vitro and in vivo (pp574 – 581) by F Ulrich Hartl & Manajit Hayer-Hartl
• An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms (pp582 – 588) by Alice I Bartlett & Sheena E Radford
• The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins (pp589 – 597) by Günter Kramer, Daniel Boehringer, Nenad Ban & Bernd Bukau
• Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI⁺] (pp598 – 605) by Peter M Tessier & Susan Lindquist
• Cellular mechanisms of membrane protein folding  (pp606 – 612)  byWilliam R Skach

…and speaking of protein folding, here are a couple of web-based resources for you to check out:

• FOLD-RATE predicts the folding rate of two and three-state proteins with/without structural class information. Read more here: FOLD-RATE — prediction of protein folding rates from amino acid sequence
• FoldX is a a computer algorithm which provides a fast and quantitative estimation of the importance of the interactions contributing to the stability of proteins and protein complexes. Read more here: The FoldX web server: an online force field
• The Protein Folding Database (PFD) is a searchable collection of all biophysical data relating to experimental protein folding studies.  Read more here: PFD: a database for the investigation of protein folding kinetics and stability
• KineticDB is a curated database of protein folding kinetics which contains currently experiments on 87 unique proteins and hundred of mutants. The main goal of KineticDB is to provide users with the diverse set of protein folding rates known from experiment. Read more here: KineticDB: a database of protein folding kinetics
• The REFOLD Database – A large number of recombinant proteins expressed in bacteria are insoluble and thus require renaturation. Identifying optimal conditions and methodology for refolding can be time consuming and often rate-limiting. To this end, REFOLD was designed to assist in the design and implementation of methodologies for the in vitro refolding of proteins. Read more here: The Matrix Refolded, REFOLD: An analytical database of protein refolding methods, and The REFOLD database: a tool for the optimization of protein expression and refolding.

To find more databases:

• OBRC: Online Bioinformatics Resources Collection – Health Sciences Library System, University of Pittsburgh
• 2009 NAR Database Summary Papers Category List

Other protein folding resources on the web:

• MIT Open Course Ware: Protein Folding Problem and Protein Folding, Misfolding and Human Disease (check out the readings section)
• Protein folding – Wikipedia
• Folding@home – a distributed computing project — people from throughout the world download and run software to band together to make one of the largest supercomputers in the world. Folding@home uses novel computational methods coupled to distributed computing, to simulate problems millions of times more challenging than previously achieved.
• Rosetta@home - a distributed computing project to determine the 3-dimensional shapes of proteins in research that may ultimately lead to finding cures for some major human diseases.  Read the Quick Guide to Rosetta@home and Its Graphics and Rosetta@home Science FAQ
• Faster Protein Folding Achieved Through Nanosecond Pressure Jump
• HHMI News: Researchers Launch Online Protein Folding Game
• foldit is a computer game enabling you to contribute to important scientific research. Read more…