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

by: RG Smock, LM Gierasch

Cell, Vol. 122, No. 6. (23 September 2005), pp. 832-834.

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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.

@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}, doi = {10.1016/j.cell.2005.09.005}, issn = {0092-8674}, journal = {Cell}, keywords = {caig, proteinfolding, protein-structure, 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} }

RIS record

TY - JOUR ID - citeulike:471650 L3 - citeulike-article-id:471650 TI - Finding the fittest fold: using the evolutionary record to design new proteins. JF - Cell VL - 122 IS - 6 SP - 832 EP - 834 AD - Department of Biochemistry & Molecular Biology, University of Massachusetts Amherst, 01003, USA. SN - 0092-8674 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. KW - caig KW - proteinfolding KW - protein-structure 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 -

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