Nice to see such a frank admission of ignorance...

from dictionary.com: ig·no·rance
   [ig-ner-uhns]
noun
the state or fact of being ignorant; lack of knowledge, learning, information, etc.

pretty standard word, I think

http://www.sciencecodex.com/read/physicists_m..._of_protein_folding-80503

Physicists at the Technische Universitaet Muenchen (TUM) are opening a new window into the life of biological cells, using a technique that lets them grab the ends of a single protein molecule and pull, making continuous, direct measurements as it unfolds and refolds. Their latest results, reported in the journal Science, reveal a complex network of intermediate structural and kinetic states along the way to functionally correct folded forms, including both express routes and dead ends. [...] Where X-ray structural analyses offer "snapshots" of protein folding, single-molecule force spectroscopy [...] produces views that are, by comparison, more like movies. Even though these movies are very "blurred," since they only capture the length of the molecule, they allow the researchers to study the dynamics of the folding process. [... using] ultra-stable, high-resolution "optical tweezers," a tool that traps miniscule objects between opposing laser beams as surely as if they were being held between thumb and forefinger. To get a grip on a calmodulin molecule, the researchers first would insert it between two molecules of a mechanically tougher protein called ubiquitin. Residues of the amino acid cysteine at the outer ends of this assembly allowed "handles" made of DNA to be attached, and these were fixed to glass beads one micrometer in diameter. The beads, and thus the calmodulin molecule between them, could then be manipulated with the optical tweezers. The essence of the experiments, repeated many times over in a variety of ways, was to pull the ends of a single, folded calmodulin molecule until it straightened out and then to reduce the tension so it could fold again, constantly measuring protein length, mechanical forces and time with extreme precision. Throughout, the calmodulin molecule was kept in conditions not too different from its working environment inside a cell, an aqueous solution with a concentration of calcium ions known to favor stable folding. Statistical analysis helped to reveal what the measurements recorded. [...] The results indicate that distinct subdomains of the calmodulin molecule fold independently yet interact with others, sometimes cooperating and sometimes interfering. "Far from being a simple two-state process," Rief explains, "the folding of a calmodulin molecule takes place via a complex network of pathways in what we call its 'energy landscape.' We found that this map of kinetic states and paths between different folded forms includes dead ends -- intermediate structures that need to be undone, like unwanted knots in a rope, before the protein can assume a shape that enables it to function properly." The researchers also discovered express routes, pathways that let some domains reach their final state much more rapidly than the molecule as a whole. [...]

Is this the right place? Another blown opportunity to boost WCG and BOINC.

http://sciencesprings.wordpress.com/2011/12/0...portunity-to-boost-boinc/

www.sciencedaily.com/releases/2012/06/120612145139.htm

Rice University researchers have developed DCA-fold, a method that uses correlations between amino acids (i.e., amino acids which apparently fold together (at the same time) but are located apart (at different locations on the same protein) to speed up the process of protein-folding computation.