Finding the fittest fold: using the evolutionary record to design new proteins. Export

@article{citeulike:471650, abstract = {For many years, the holy grail of protein engineering has been the design of artificial amino acid sequences that fold into stable proteins with desired functions. In the current issue of Nature, two papers from the Ranganathan group (Russ et al., 2005; Socolich et al., 2005) report remarkable success in the design of artificial WW domains. Their method, termed statistical coupling analysis (Lockless and Ranganathan, 1999), does not use structural or physicochemical information but instead extracts information about essential patterns of amino acids from the evolutionary record.}, address = {Department of Biochemistry \& Molecular Biology, University of Massachusetts Amherst, 01003, USA.}, author = {Smock, R. G. and Gierasch, L. M.}, citeulike-article-id = {471650}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2005.09.005}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16179253}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16179253}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6WSN-4H5F9G4-8/2/fe26db13bb73c1f3f5a117e15fc7ee8c}, doi = {10.1016/j.cell.2005.09.005}, issn = {0092-8674}, journal = {Cell}, keywords = {caig, protein-structure, proteinfolding, residue-covariation}, month = {September}, number = {6}, pages = {832--834}, posted-at = {2006-07-05 08:27:59}, priority = {0}, title = {Finding the fittest fold: using the evolutionary record to design new proteins.}, url = {http://dx.doi.org/10.1016/j.cell.2005.09.005}, volume = {122}, year = {2005} }

TY - JOUR ID - citeulike:471650 L3 - citeulike-article-id:471650 N2 - For many years, the holy grail of protein engineering has been the design of artificial amino acid sequences that fold into stable proteins with desired functions. In the current issue of Nature, two papers from the Ranganathan group (Russ et al., 2005; Socolich et al., 2005) report remarkable success in the design of artificial WW domains. Their method, termed statistical coupling analysis (Lockless and Ranganathan, 1999), does not use structural or physicochemical information but instead extracts information about essential patterns of amino acids from the evolutionary record. IS - 6 JF - Cell SN - 0092-8674 AD - Department of Biochemistry & Molecular Biology, University of Massachusetts Amherst, 01003, USA. EP - 834 TI - Finding the fittest fold: using the evolutionary record to design new proteins. VL - 122 SP - 832 KW - caig KW - protein-structure KW - proteinfolding KW - residue-covariation AU - Smock, RG AU - Gierasch, LM PY - 2005/09/23/ UR - http://dx.doi.org/10.1016/j.cell.2005.09.005 ER -