Engineering of zinc finger and MHC motifs to locked-in tertiary folds

The assembly of helical and b-sheet peptide blocks contg. reactive chain ends results in highly branched chain architectures (\"locked-in folds\") mimicking native tertiary structures. This mol. kit strategy allows to bypass the protein folding problem in protein de novo design and gives access to protein mimetics of high thermo-dynamic stability. The validity of this concept is exemplified for the design and synthesis of locked-in folds mimicking the zinc finger and MHC folding motifs. [on SciFinder (R)]


Published in:
Letters in Peptide Science, 4, 2, 95-100
Year:
1997
Laboratories:




 Record created 2006-02-09, last modified 2018-01-27


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)