Inverse protein folding

How to design sequences tliat adopt a specified fold [9] This is tire inverse protein folding problem tliat is vital to the biotechnology industry. There are some proteins tliat do not spontaneously reach tire native confomiation. In tire cells tliese proteins fold witli tire assistance of helper molecules referred to as chaperonins. The chaperonin-mediated folding problem involves an understanding of tire interactions between proteins. 

A Godzik, A Kolinski, J Skolmck. Topology fingerprint approach to the inverse protein folding problem. J Mol Biol 227 227-238, 1992. 

The Inverse Protein Folding Problem Protein Design and Structure Prediction in the Genomic Era... 

M. Wilmanns, D. Eisenberg. Inverse protein folding by the residue pair preference profile method estimating the correctness of alignments of structurally compatibile sequences. Prot. Eng. 1995, 8, 627-639. 

Molecular modeling is also used in protein engineering to modify specifically or randomly selected residues of a protein to change the substrate specificity or to try to find an amino acid sequence that will fold into a specific, preselected 3D shape (the inverse protein folding problem). An introduction to this topic has been written by van Gunsteren. xhe principles of modeling have also been used to design new enzymes with altered substrate specificity. - ... 

How to design sequenees that adopt a speeified fold [9] This is the inverse protein folding problem that is vital to the bioteehnology industry. There are some proteins that do not spontaneously reaeh the native eonformation. In the eells these proteins fold with the assistanee of helper moleeules referred to as ehaperonins. The ehaperonin-mediated folding problem involves an understanding of the interaetions between proteins. 

T. M. A. Fink, Inverse Protein Folding, Hierarchical Optimisation and Tie Knots, Dissertation, University of Cambridge, Cambridge, 1998. 

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